Two conformations of a crystalline human tRNA synthetase–tRNA complex: implications for protein synthesis
Abstract Aminoacylation of tRNA is the first step of protein synthesis. Here, we report the co‐crystal structure of human tryptophanyl‐tRNA synthetase and $ tRNA^{Trp} $. This enzyme is reported to interact directly with elongation factor 1α, which carries charged tRNA to the ribosome. Crystals were...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Yang, Xiang‐Lei [verfasserIn] Otero, Francella J [verfasserIn] Ewalt, Karla L [verfasserIn] Liu, Jianming [verfasserIn] Swairjo, Manal A [verfasserIn] Köhrer, Caroline [verfasserIn] RajBhandary, Uttam L [verfasserIn] Skene, Robert J [verfasserIn] McRee, Duncan E [verfasserIn] Schimmel, Paul [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2006 |
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| Schlagwörter: |
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| Anmerkung: |
© European Molecular Biology Organization 2006 |
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| Übergeordnetes Werk: |
Enthalten in: The EMBO Journal - Nature Publishing Group UK, 2023, 25(2006), 12 vom: 25. Mai, Seite 2919-2929 |
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| Übergeordnetes Werk: |
volume:25 ; year:2006 ; number:12 ; day:25 ; month:05 ; pages:2919-2929 |
| Links: |
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| DOI / URN: |
10.1038/sj.emboj.7601154 |
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| Katalog-ID: |
SPR057951985 |
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| 100 | 1 | |a Yang, Xiang‐Lei |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Two conformations of a crystalline human tRNA synthetase–tRNA complex: implications for protein synthesis |
| 264 | 1 | |c 2006 | |
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| 520 | |a Abstract Aminoacylation of tRNA is the first step of protein synthesis. Here, we report the co‐crystal structure of human tryptophanyl‐tRNA synthetase and $ tRNA^{Trp} $. This enzyme is reported to interact directly with elongation factor 1α, which carries charged tRNA to the ribosome. Crystals were generated from a 50/50% mixture of charged and uncharged $ tRNA^{Trp} $. These crystals captured two conformations of the complex, which are nearly identical with respect to the protein and a bound tryptophan. They are distinguished by the way tRNA is bound. In one, uncharged tRNA is bound across the dimer, with anticodon and acceptor stem interacting with separate subunits. In this cross‐dimer tRNA complex, the class I enzyme has a class II‐like tRNA binding mode. This structure accounts for biochemical investigations of human TrpRS, including species‐specific charging. In the other conformation, presumptive aminoacylated tRNA is bound only by the anticodon, the acceptor stem being free and having space to interact precisely with EF‐1α, suggesting that the product of aminoacylation can be directly handed off to EF‐1α for the next step of protein synthesis. | ||
| 650 | 4 | |a aminoacyl‐tRNA synthetase |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a crystal structure |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a dual conformations |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a human TrpRS |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a tRNA |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Otero, Francella J |e verfasserin |4 aut | |
| 700 | 1 | |a Ewalt, Karla L |e verfasserin |4 aut | |
| 700 | 1 | |a Liu, Jianming |e verfasserin |4 aut | |
| 700 | 1 | |a Swairjo, Manal A |e verfasserin |4 aut | |
| 700 | 1 | |a Köhrer, Caroline |e verfasserin |4 aut | |
| 700 | 1 | |a RajBhandary, Uttam L |e verfasserin |4 aut | |
| 700 | 1 | |a Skene, Robert J |e verfasserin |4 aut | |
| 700 | 1 | |a McRee, Duncan E |e verfasserin |4 aut | |
| 700 | 1 | |a Schimmel, Paul |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t The EMBO Journal |d Nature Publishing Group UK, 2023 |g 25(2006), 12 vom: 25. Mai, Seite 2919-2929 |w (DE-627)266022529 |w (DE-600)1467419-1 |x 1460-2075 |7 nnns |
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10.1038/sj.emboj.7601154 doi (DE-627)SPR057951985 (SPR)sj.emboj.7601154-e DE-627 ger DE-627 rakwb eng Yang, Xiang‐Lei verfasserin aut Two conformations of a crystalline human tRNA synthetase–tRNA complex: implications for protein synthesis 2006 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2006 Abstract Aminoacylation of tRNA is the first step of protein synthesis. Here, we report the co‐crystal structure of human tryptophanyl‐tRNA synthetase and $ tRNA^{Trp} $. This enzyme is reported to interact directly with elongation factor 1α, which carries charged tRNA to the ribosome. Crystals were generated from a 50/50% mixture of charged and uncharged $ tRNA^{Trp} $. These crystals captured two conformations of the complex, which are nearly identical with respect to the protein and a bound tryptophan. They are distinguished by the way tRNA is bound. In one, uncharged tRNA is bound across the dimer, with anticodon and acceptor stem interacting with separate subunits. In this cross‐dimer tRNA complex, the class I enzyme has a class II‐like tRNA binding mode. This structure accounts for biochemical investigations of human TrpRS, including species‐specific charging. In the other conformation, presumptive aminoacylated tRNA is bound only by the anticodon, the acceptor stem being free and having space to interact precisely with EF‐1α, suggesting that the product of aminoacylation can be directly handed off to EF‐1α for the next step of protein synthesis. aminoacyl‐tRNA synthetase (dpeaa)DE-He213 crystal structure (dpeaa)DE-He213 dual conformations (dpeaa)DE-He213 human TrpRS (dpeaa)DE-He213 tRNA (dpeaa)DE-He213 Otero, Francella J verfasserin aut Ewalt, Karla L verfasserin aut Liu, Jianming verfasserin aut Swairjo, Manal A verfasserin aut Köhrer, Caroline verfasserin aut RajBhandary, Uttam L verfasserin aut Skene, Robert J verfasserin aut McRee, Duncan E verfasserin aut Schimmel, Paul verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 25(2006), 12 vom: 25. Mai, Seite 2919-2929 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:25 year:2006 number:12 day:25 month:05 pages:2919-2929 https://dx.doi.org/10.1038/sj.emboj.7601154 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 25 2006 12 25 05 2919-2929 |
| spelling |
10.1038/sj.emboj.7601154 doi (DE-627)SPR057951985 (SPR)sj.emboj.7601154-e DE-627 ger DE-627 rakwb eng Yang, Xiang‐Lei verfasserin aut Two conformations of a crystalline human tRNA synthetase–tRNA complex: implications for protein synthesis 2006 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2006 Abstract Aminoacylation of tRNA is the first step of protein synthesis. Here, we report the co‐crystal structure of human tryptophanyl‐tRNA synthetase and $ tRNA^{Trp} $. This enzyme is reported to interact directly with elongation factor 1α, which carries charged tRNA to the ribosome. Crystals were generated from a 50/50% mixture of charged and uncharged $ tRNA^{Trp} $. These crystals captured two conformations of the complex, which are nearly identical with respect to the protein and a bound tryptophan. They are distinguished by the way tRNA is bound. In one, uncharged tRNA is bound across the dimer, with anticodon and acceptor stem interacting with separate subunits. In this cross‐dimer tRNA complex, the class I enzyme has a class II‐like tRNA binding mode. This structure accounts for biochemical investigations of human TrpRS, including species‐specific charging. In the other conformation, presumptive aminoacylated tRNA is bound only by the anticodon, the acceptor stem being free and having space to interact precisely with EF‐1α, suggesting that the product of aminoacylation can be directly handed off to EF‐1α for the next step of protein synthesis. aminoacyl‐tRNA synthetase (dpeaa)DE-He213 crystal structure (dpeaa)DE-He213 dual conformations (dpeaa)DE-He213 human TrpRS (dpeaa)DE-He213 tRNA (dpeaa)DE-He213 Otero, Francella J verfasserin aut Ewalt, Karla L verfasserin aut Liu, Jianming verfasserin aut Swairjo, Manal A verfasserin aut Köhrer, Caroline verfasserin aut RajBhandary, Uttam L verfasserin aut Skene, Robert J verfasserin aut McRee, Duncan E verfasserin aut Schimmel, Paul verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 25(2006), 12 vom: 25. Mai, Seite 2919-2929 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:25 year:2006 number:12 day:25 month:05 pages:2919-2929 https://dx.doi.org/10.1038/sj.emboj.7601154 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 25 2006 12 25 05 2919-2929 |
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10.1038/sj.emboj.7601154 doi (DE-627)SPR057951985 (SPR)sj.emboj.7601154-e DE-627 ger DE-627 rakwb eng Yang, Xiang‐Lei verfasserin aut Two conformations of a crystalline human tRNA synthetase–tRNA complex: implications for protein synthesis 2006 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2006 Abstract Aminoacylation of tRNA is the first step of protein synthesis. Here, we report the co‐crystal structure of human tryptophanyl‐tRNA synthetase and $ tRNA^{Trp} $. This enzyme is reported to interact directly with elongation factor 1α, which carries charged tRNA to the ribosome. Crystals were generated from a 50/50% mixture of charged and uncharged $ tRNA^{Trp} $. These crystals captured two conformations of the complex, which are nearly identical with respect to the protein and a bound tryptophan. They are distinguished by the way tRNA is bound. In one, uncharged tRNA is bound across the dimer, with anticodon and acceptor stem interacting with separate subunits. In this cross‐dimer tRNA complex, the class I enzyme has a class II‐like tRNA binding mode. This structure accounts for biochemical investigations of human TrpRS, including species‐specific charging. In the other conformation, presumptive aminoacylated tRNA is bound only by the anticodon, the acceptor stem being free and having space to interact precisely with EF‐1α, suggesting that the product of aminoacylation can be directly handed off to EF‐1α for the next step of protein synthesis. aminoacyl‐tRNA synthetase (dpeaa)DE-He213 crystal structure (dpeaa)DE-He213 dual conformations (dpeaa)DE-He213 human TrpRS (dpeaa)DE-He213 tRNA (dpeaa)DE-He213 Otero, Francella J verfasserin aut Ewalt, Karla L verfasserin aut Liu, Jianming verfasserin aut Swairjo, Manal A verfasserin aut Köhrer, Caroline verfasserin aut RajBhandary, Uttam L verfasserin aut Skene, Robert J verfasserin aut McRee, Duncan E verfasserin aut Schimmel, Paul verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 25(2006), 12 vom: 25. Mai, Seite 2919-2929 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:25 year:2006 number:12 day:25 month:05 pages:2919-2929 https://dx.doi.org/10.1038/sj.emboj.7601154 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 25 2006 12 25 05 2919-2929 |
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10.1038/sj.emboj.7601154 doi (DE-627)SPR057951985 (SPR)sj.emboj.7601154-e DE-627 ger DE-627 rakwb eng Yang, Xiang‐Lei verfasserin aut Two conformations of a crystalline human tRNA synthetase–tRNA complex: implications for protein synthesis 2006 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2006 Abstract Aminoacylation of tRNA is the first step of protein synthesis. Here, we report the co‐crystal structure of human tryptophanyl‐tRNA synthetase and $ tRNA^{Trp} $. This enzyme is reported to interact directly with elongation factor 1α, which carries charged tRNA to the ribosome. Crystals were generated from a 50/50% mixture of charged and uncharged $ tRNA^{Trp} $. These crystals captured two conformations of the complex, which are nearly identical with respect to the protein and a bound tryptophan. They are distinguished by the way tRNA is bound. In one, uncharged tRNA is bound across the dimer, with anticodon and acceptor stem interacting with separate subunits. In this cross‐dimer tRNA complex, the class I enzyme has a class II‐like tRNA binding mode. This structure accounts for biochemical investigations of human TrpRS, including species‐specific charging. In the other conformation, presumptive aminoacylated tRNA is bound only by the anticodon, the acceptor stem being free and having space to interact precisely with EF‐1α, suggesting that the product of aminoacylation can be directly handed off to EF‐1α for the next step of protein synthesis. aminoacyl‐tRNA synthetase (dpeaa)DE-He213 crystal structure (dpeaa)DE-He213 dual conformations (dpeaa)DE-He213 human TrpRS (dpeaa)DE-He213 tRNA (dpeaa)DE-He213 Otero, Francella J verfasserin aut Ewalt, Karla L verfasserin aut Liu, Jianming verfasserin aut Swairjo, Manal A verfasserin aut Köhrer, Caroline verfasserin aut RajBhandary, Uttam L verfasserin aut Skene, Robert J verfasserin aut McRee, Duncan E verfasserin aut Schimmel, Paul verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 25(2006), 12 vom: 25. Mai, Seite 2919-2929 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:25 year:2006 number:12 day:25 month:05 pages:2919-2929 https://dx.doi.org/10.1038/sj.emboj.7601154 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 25 2006 12 25 05 2919-2929 |
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10.1038/sj.emboj.7601154 doi (DE-627)SPR057951985 (SPR)sj.emboj.7601154-e DE-627 ger DE-627 rakwb eng Yang, Xiang‐Lei verfasserin aut Two conformations of a crystalline human tRNA synthetase–tRNA complex: implications for protein synthesis 2006 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2006 Abstract Aminoacylation of tRNA is the first step of protein synthesis. Here, we report the co‐crystal structure of human tryptophanyl‐tRNA synthetase and $ tRNA^{Trp} $. This enzyme is reported to interact directly with elongation factor 1α, which carries charged tRNA to the ribosome. Crystals were generated from a 50/50% mixture of charged and uncharged $ tRNA^{Trp} $. These crystals captured two conformations of the complex, which are nearly identical with respect to the protein and a bound tryptophan. They are distinguished by the way tRNA is bound. In one, uncharged tRNA is bound across the dimer, with anticodon and acceptor stem interacting with separate subunits. In this cross‐dimer tRNA complex, the class I enzyme has a class II‐like tRNA binding mode. This structure accounts for biochemical investigations of human TrpRS, including species‐specific charging. In the other conformation, presumptive aminoacylated tRNA is bound only by the anticodon, the acceptor stem being free and having space to interact precisely with EF‐1α, suggesting that the product of aminoacylation can be directly handed off to EF‐1α for the next step of protein synthesis. aminoacyl‐tRNA synthetase (dpeaa)DE-He213 crystal structure (dpeaa)DE-He213 dual conformations (dpeaa)DE-He213 human TrpRS (dpeaa)DE-He213 tRNA (dpeaa)DE-He213 Otero, Francella J verfasserin aut Ewalt, Karla L verfasserin aut Liu, Jianming verfasserin aut Swairjo, Manal A verfasserin aut Köhrer, Caroline verfasserin aut RajBhandary, Uttam L verfasserin aut Skene, Robert J verfasserin aut McRee, Duncan E verfasserin aut Schimmel, Paul verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 25(2006), 12 vom: 25. Mai, Seite 2919-2929 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:25 year:2006 number:12 day:25 month:05 pages:2919-2929 https://dx.doi.org/10.1038/sj.emboj.7601154 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 25 2006 12 25 05 2919-2929 |
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Yang, Xiang‐Lei @@aut@@ Otero, Francella J @@aut@@ Ewalt, Karla L @@aut@@ Liu, Jianming @@aut@@ Swairjo, Manal A @@aut@@ Köhrer, Caroline @@aut@@ RajBhandary, Uttam L @@aut@@ Skene, Robert J @@aut@@ McRee, Duncan E @@aut@@ Schimmel, Paul @@aut@@ |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000naa a22002652 4500</leader><controlfield tag="001">SPR057951985</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20241022064912.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">241022s2006 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1038/sj.emboj.7601154</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR057951985</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)sj.emboj.7601154-e</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Yang, Xiang‐Lei</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Two conformations of a crystalline human tRNA synthetase–tRNA complex: implications for protein synthesis</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2006</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">© European Molecular Biology Organization 2006</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract Aminoacylation of tRNA is the first step of protein synthesis. Here, we report the co‐crystal structure of human tryptophanyl‐tRNA synthetase and $ tRNA^{Trp} $. This enzyme is reported to interact directly with elongation factor 1α, which carries charged tRNA to the ribosome. Crystals were generated from a 50/50% mixture of charged and uncharged $ tRNA^{Trp} $. These crystals captured two conformations of the complex, which are nearly identical with respect to the protein and a bound tryptophan. They are distinguished by the way tRNA is bound. In one, uncharged tRNA is bound across the dimer, with anticodon and acceptor stem interacting with separate subunits. In this cross‐dimer tRNA complex, the class I enzyme has a class II‐like tRNA binding mode. This structure accounts for biochemical investigations of human TrpRS, including species‐specific charging. 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Yang, Xiang‐Lei |
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Yang, Xiang‐Lei misc aminoacyl‐tRNA synthetase misc crystal structure misc dual conformations misc human TrpRS misc tRNA Two conformations of a crystalline human tRNA synthetase–tRNA complex: implications for protein synthesis |
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Two conformations of a crystalline human tRNA synthetase–tRNA complex: implications for protein synthesis aminoacyl‐tRNA synthetase (dpeaa)DE-He213 crystal structure (dpeaa)DE-He213 dual conformations (dpeaa)DE-He213 human TrpRS (dpeaa)DE-He213 tRNA (dpeaa)DE-He213 |
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Two conformations of a crystalline human tRNA synthetase–tRNA complex: implications for protein synthesis |
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Yang, Xiang‐Lei Otero, Francella J Ewalt, Karla L Liu, Jianming Swairjo, Manal A Köhrer, Caroline RajBhandary, Uttam L Skene, Robert J McRee, Duncan E Schimmel, Paul |
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two conformations of a crystalline human trna synthetase–trna complex: implications for protein synthesis |
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Two conformations of a crystalline human tRNA synthetase–tRNA complex: implications for protein synthesis |
| abstract |
Abstract Aminoacylation of tRNA is the first step of protein synthesis. Here, we report the co‐crystal structure of human tryptophanyl‐tRNA synthetase and $ tRNA^{Trp} $. This enzyme is reported to interact directly with elongation factor 1α, which carries charged tRNA to the ribosome. Crystals were generated from a 50/50% mixture of charged and uncharged $ tRNA^{Trp} $. These crystals captured two conformations of the complex, which are nearly identical with respect to the protein and a bound tryptophan. They are distinguished by the way tRNA is bound. In one, uncharged tRNA is bound across the dimer, with anticodon and acceptor stem interacting with separate subunits. In this cross‐dimer tRNA complex, the class I enzyme has a class II‐like tRNA binding mode. This structure accounts for biochemical investigations of human TrpRS, including species‐specific charging. In the other conformation, presumptive aminoacylated tRNA is bound only by the anticodon, the acceptor stem being free and having space to interact precisely with EF‐1α, suggesting that the product of aminoacylation can be directly handed off to EF‐1α for the next step of protein synthesis. © European Molecular Biology Organization 2006 |
| abstractGer |
Abstract Aminoacylation of tRNA is the first step of protein synthesis. Here, we report the co‐crystal structure of human tryptophanyl‐tRNA synthetase and $ tRNA^{Trp} $. This enzyme is reported to interact directly with elongation factor 1α, which carries charged tRNA to the ribosome. Crystals were generated from a 50/50% mixture of charged and uncharged $ tRNA^{Trp} $. These crystals captured two conformations of the complex, which are nearly identical with respect to the protein and a bound tryptophan. They are distinguished by the way tRNA is bound. In one, uncharged tRNA is bound across the dimer, with anticodon and acceptor stem interacting with separate subunits. In this cross‐dimer tRNA complex, the class I enzyme has a class II‐like tRNA binding mode. This structure accounts for biochemical investigations of human TrpRS, including species‐specific charging. In the other conformation, presumptive aminoacylated tRNA is bound only by the anticodon, the acceptor stem being free and having space to interact precisely with EF‐1α, suggesting that the product of aminoacylation can be directly handed off to EF‐1α for the next step of protein synthesis. © European Molecular Biology Organization 2006 |
| abstract_unstemmed |
Abstract Aminoacylation of tRNA is the first step of protein synthesis. Here, we report the co‐crystal structure of human tryptophanyl‐tRNA synthetase and $ tRNA^{Trp} $. This enzyme is reported to interact directly with elongation factor 1α, which carries charged tRNA to the ribosome. Crystals were generated from a 50/50% mixture of charged and uncharged $ tRNA^{Trp} $. These crystals captured two conformations of the complex, which are nearly identical with respect to the protein and a bound tryptophan. They are distinguished by the way tRNA is bound. In one, uncharged tRNA is bound across the dimer, with anticodon and acceptor stem interacting with separate subunits. In this cross‐dimer tRNA complex, the class I enzyme has a class II‐like tRNA binding mode. This structure accounts for biochemical investigations of human TrpRS, including species‐specific charging. In the other conformation, presumptive aminoacylated tRNA is bound only by the anticodon, the acceptor stem being free and having space to interact precisely with EF‐1α, suggesting that the product of aminoacylation can be directly handed off to EF‐1α for the next step of protein synthesis. © European Molecular Biology Organization 2006 |
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| title_short |
Two conformations of a crystalline human tRNA synthetase–tRNA complex: implications for protein synthesis |
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https://dx.doi.org/10.1038/sj.emboj.7601154 |
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Otero, Francella J Ewalt, Karla L Liu, Jianming Swairjo, Manal A Köhrer, Caroline RajBhandary, Uttam L Skene, Robert J McRee, Duncan E Schimmel, Paul |
| author2Str |
Otero, Francella J Ewalt, Karla L Liu, Jianming Swairjo, Manal A Köhrer, Caroline RajBhandary, Uttam L Skene, Robert J McRee, Duncan E Schimmel, Paul |
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| score |
7.3993473 |