Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3
Abstract The small ribosomal subunit is responsible for the decoding of genetic information and plays a key role in the initiation of protein synthesis. We analyzed by X‐ray crystallography the structures of three different complexes of the small ribosomal subunit of Thermus thermophilus with the A‐...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Pioletti, Marta [verfasserIn] Schlünzen, Frank [verfasserIn] Harms, Jörg [verfasserIn] Zarivach, Raz [verfasserIn] Glühmann, Marco [verfasserIn] Avila, Horacio [verfasserIn] Bashan, Anat [verfasserIn] Bartels, Heike [verfasserIn] Auerbach, Tamar [verfasserIn] Jacobi, Carsten [verfasserIn] Hartsch, Thomas [verfasserIn] Yonath, Ada [verfasserIn] Franceschi, François [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2001 |
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| Schlagwörter: |
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| Anmerkung: |
© European Molecular Biology Organization 2001 |
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| Übergeordnetes Werk: |
Enthalten in: The EMBO Journal - Nature Publishing Group UK, 2023, 20(2001), 8 vom: 17. Apr., Seite 1829-1839 |
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| Übergeordnetes Werk: |
volume:20 ; year:2001 ; number:8 ; day:17 ; month:04 ; pages:1829-1839 |
| Links: |
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| DOI / URN: |
10.1093/emboj/20.8.1829 |
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| Katalog-ID: |
SPR057946183 |
|---|
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| 041 | |a eng | ||
| 100 | 1 | |a Pioletti, Marta |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3 |
| 264 | 1 | |c 2001 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a Computermedien |b c |2 rdamedia | ||
| 338 | |a Online-Ressource |b cr |2 rdacarrier | ||
| 500 | |a © European Molecular Biology Organization 2001 | ||
| 520 | |a Abstract The small ribosomal subunit is responsible for the decoding of genetic information and plays a key role in the initiation of protein synthesis. We analyzed by X‐ray crystallography the structures of three different complexes of the small ribosomal subunit of Thermus thermophilus with the A‐site inhibitor tetracycline, the universal initiation inhibitor edeine and the C‐terminal domain of the translation initiation factor IF3. The crystal structure analysis of the complex with tetracycline revealed the functionally important site responsible for the blockage of the A‐site. Five additional tetracycline sites resolve most of the controversial biochemical data on the location of tetracycline. The interaction of edeine with the small subunit indicates its role in inhibiting initiation and shows its involvement with P‐site tRNA. The location of the C‐terminal domain of IF3, at the solvent side of the platform, sheds light on the formation of the initiation complex, and implies that the anti‐association activity of IF3 is due to its influence on the conformational dynamics of the small ribosomal subunit. | ||
| 650 | 4 | |a antibiotics |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a edeine |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a IF3 |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a ribosomes |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a tetracycline |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Schlünzen, Frank |e verfasserin |4 aut | |
| 700 | 1 | |a Harms, Jörg |e verfasserin |4 aut | |
| 700 | 1 | |a Zarivach, Raz |e verfasserin |4 aut | |
| 700 | 1 | |a Glühmann, Marco |e verfasserin |4 aut | |
| 700 | 1 | |a Avila, Horacio |e verfasserin |4 aut | |
| 700 | 1 | |a Bashan, Anat |e verfasserin |4 aut | |
| 700 | 1 | |a Bartels, Heike |e verfasserin |4 aut | |
| 700 | 1 | |a Auerbach, Tamar |e verfasserin |4 aut | |
| 700 | 1 | |a Jacobi, Carsten |e verfasserin |4 aut | |
| 700 | 1 | |a Hartsch, Thomas |e verfasserin |4 aut | |
| 700 | 1 | |a Yonath, Ada |e verfasserin |4 aut | |
| 700 | 1 | |a Franceschi, François |e verfasserin |4 aut | |
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| 952 | |d 20 |j 2001 |e 8 |b 17 |c 04 |h 1829-1839 | ||
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2001 |
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2001 |
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10.1093/emboj/20.8.1829 doi (DE-627)SPR057946183 (SPR)20.8.1829-e DE-627 ger DE-627 rakwb eng Pioletti, Marta verfasserin aut Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3 2001 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2001 Abstract The small ribosomal subunit is responsible for the decoding of genetic information and plays a key role in the initiation of protein synthesis. We analyzed by X‐ray crystallography the structures of three different complexes of the small ribosomal subunit of Thermus thermophilus with the A‐site inhibitor tetracycline, the universal initiation inhibitor edeine and the C‐terminal domain of the translation initiation factor IF3. The crystal structure analysis of the complex with tetracycline revealed the functionally important site responsible for the blockage of the A‐site. Five additional tetracycline sites resolve most of the controversial biochemical data on the location of tetracycline. The interaction of edeine with the small subunit indicates its role in inhibiting initiation and shows its involvement with P‐site tRNA. The location of the C‐terminal domain of IF3, at the solvent side of the platform, sheds light on the formation of the initiation complex, and implies that the anti‐association activity of IF3 is due to its influence on the conformational dynamics of the small ribosomal subunit. antibiotics (dpeaa)DE-He213 edeine (dpeaa)DE-He213 IF3 (dpeaa)DE-He213 ribosomes (dpeaa)DE-He213 tetracycline (dpeaa)DE-He213 Schlünzen, Frank verfasserin aut Harms, Jörg verfasserin aut Zarivach, Raz verfasserin aut Glühmann, Marco verfasserin aut Avila, Horacio verfasserin aut Bashan, Anat verfasserin aut Bartels, Heike verfasserin aut Auerbach, Tamar verfasserin aut Jacobi, Carsten verfasserin aut Hartsch, Thomas verfasserin aut Yonath, Ada verfasserin aut Franceschi, François verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 20(2001), 8 vom: 17. Apr., Seite 1829-1839 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:20 year:2001 number:8 day:17 month:04 pages:1829-1839 https://dx.doi.org/10.1093/emboj/20.8.1829 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 20 2001 8 17 04 1829-1839 |
| spelling |
10.1093/emboj/20.8.1829 doi (DE-627)SPR057946183 (SPR)20.8.1829-e DE-627 ger DE-627 rakwb eng Pioletti, Marta verfasserin aut Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3 2001 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2001 Abstract The small ribosomal subunit is responsible for the decoding of genetic information and plays a key role in the initiation of protein synthesis. We analyzed by X‐ray crystallography the structures of three different complexes of the small ribosomal subunit of Thermus thermophilus with the A‐site inhibitor tetracycline, the universal initiation inhibitor edeine and the C‐terminal domain of the translation initiation factor IF3. The crystal structure analysis of the complex with tetracycline revealed the functionally important site responsible for the blockage of the A‐site. Five additional tetracycline sites resolve most of the controversial biochemical data on the location of tetracycline. The interaction of edeine with the small subunit indicates its role in inhibiting initiation and shows its involvement with P‐site tRNA. The location of the C‐terminal domain of IF3, at the solvent side of the platform, sheds light on the formation of the initiation complex, and implies that the anti‐association activity of IF3 is due to its influence on the conformational dynamics of the small ribosomal subunit. antibiotics (dpeaa)DE-He213 edeine (dpeaa)DE-He213 IF3 (dpeaa)DE-He213 ribosomes (dpeaa)DE-He213 tetracycline (dpeaa)DE-He213 Schlünzen, Frank verfasserin aut Harms, Jörg verfasserin aut Zarivach, Raz verfasserin aut Glühmann, Marco verfasserin aut Avila, Horacio verfasserin aut Bashan, Anat verfasserin aut Bartels, Heike verfasserin aut Auerbach, Tamar verfasserin aut Jacobi, Carsten verfasserin aut Hartsch, Thomas verfasserin aut Yonath, Ada verfasserin aut Franceschi, François verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 20(2001), 8 vom: 17. Apr., Seite 1829-1839 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:20 year:2001 number:8 day:17 month:04 pages:1829-1839 https://dx.doi.org/10.1093/emboj/20.8.1829 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 20 2001 8 17 04 1829-1839 |
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10.1093/emboj/20.8.1829 doi (DE-627)SPR057946183 (SPR)20.8.1829-e DE-627 ger DE-627 rakwb eng Pioletti, Marta verfasserin aut Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3 2001 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2001 Abstract The small ribosomal subunit is responsible for the decoding of genetic information and plays a key role in the initiation of protein synthesis. We analyzed by X‐ray crystallography the structures of three different complexes of the small ribosomal subunit of Thermus thermophilus with the A‐site inhibitor tetracycline, the universal initiation inhibitor edeine and the C‐terminal domain of the translation initiation factor IF3. The crystal structure analysis of the complex with tetracycline revealed the functionally important site responsible for the blockage of the A‐site. Five additional tetracycline sites resolve most of the controversial biochemical data on the location of tetracycline. The interaction of edeine with the small subunit indicates its role in inhibiting initiation and shows its involvement with P‐site tRNA. The location of the C‐terminal domain of IF3, at the solvent side of the platform, sheds light on the formation of the initiation complex, and implies that the anti‐association activity of IF3 is due to its influence on the conformational dynamics of the small ribosomal subunit. antibiotics (dpeaa)DE-He213 edeine (dpeaa)DE-He213 IF3 (dpeaa)DE-He213 ribosomes (dpeaa)DE-He213 tetracycline (dpeaa)DE-He213 Schlünzen, Frank verfasserin aut Harms, Jörg verfasserin aut Zarivach, Raz verfasserin aut Glühmann, Marco verfasserin aut Avila, Horacio verfasserin aut Bashan, Anat verfasserin aut Bartels, Heike verfasserin aut Auerbach, Tamar verfasserin aut Jacobi, Carsten verfasserin aut Hartsch, Thomas verfasserin aut Yonath, Ada verfasserin aut Franceschi, François verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 20(2001), 8 vom: 17. Apr., Seite 1829-1839 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:20 year:2001 number:8 day:17 month:04 pages:1829-1839 https://dx.doi.org/10.1093/emboj/20.8.1829 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 20 2001 8 17 04 1829-1839 |
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10.1093/emboj/20.8.1829 doi (DE-627)SPR057946183 (SPR)20.8.1829-e DE-627 ger DE-627 rakwb eng Pioletti, Marta verfasserin aut Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3 2001 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2001 Abstract The small ribosomal subunit is responsible for the decoding of genetic information and plays a key role in the initiation of protein synthesis. We analyzed by X‐ray crystallography the structures of three different complexes of the small ribosomal subunit of Thermus thermophilus with the A‐site inhibitor tetracycline, the universal initiation inhibitor edeine and the C‐terminal domain of the translation initiation factor IF3. The crystal structure analysis of the complex with tetracycline revealed the functionally important site responsible for the blockage of the A‐site. Five additional tetracycline sites resolve most of the controversial biochemical data on the location of tetracycline. The interaction of edeine with the small subunit indicates its role in inhibiting initiation and shows its involvement with P‐site tRNA. The location of the C‐terminal domain of IF3, at the solvent side of the platform, sheds light on the formation of the initiation complex, and implies that the anti‐association activity of IF3 is due to its influence on the conformational dynamics of the small ribosomal subunit. antibiotics (dpeaa)DE-He213 edeine (dpeaa)DE-He213 IF3 (dpeaa)DE-He213 ribosomes (dpeaa)DE-He213 tetracycline (dpeaa)DE-He213 Schlünzen, Frank verfasserin aut Harms, Jörg verfasserin aut Zarivach, Raz verfasserin aut Glühmann, Marco verfasserin aut Avila, Horacio verfasserin aut Bashan, Anat verfasserin aut Bartels, Heike verfasserin aut Auerbach, Tamar verfasserin aut Jacobi, Carsten verfasserin aut Hartsch, Thomas verfasserin aut Yonath, Ada verfasserin aut Franceschi, François verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 20(2001), 8 vom: 17. Apr., Seite 1829-1839 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:20 year:2001 number:8 day:17 month:04 pages:1829-1839 https://dx.doi.org/10.1093/emboj/20.8.1829 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 20 2001 8 17 04 1829-1839 |
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10.1093/emboj/20.8.1829 doi (DE-627)SPR057946183 (SPR)20.8.1829-e DE-627 ger DE-627 rakwb eng Pioletti, Marta verfasserin aut Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3 2001 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2001 Abstract The small ribosomal subunit is responsible for the decoding of genetic information and plays a key role in the initiation of protein synthesis. We analyzed by X‐ray crystallography the structures of three different complexes of the small ribosomal subunit of Thermus thermophilus with the A‐site inhibitor tetracycline, the universal initiation inhibitor edeine and the C‐terminal domain of the translation initiation factor IF3. The crystal structure analysis of the complex with tetracycline revealed the functionally important site responsible for the blockage of the A‐site. Five additional tetracycline sites resolve most of the controversial biochemical data on the location of tetracycline. The interaction of edeine with the small subunit indicates its role in inhibiting initiation and shows its involvement with P‐site tRNA. The location of the C‐terminal domain of IF3, at the solvent side of the platform, sheds light on the formation of the initiation complex, and implies that the anti‐association activity of IF3 is due to its influence on the conformational dynamics of the small ribosomal subunit. antibiotics (dpeaa)DE-He213 edeine (dpeaa)DE-He213 IF3 (dpeaa)DE-He213 ribosomes (dpeaa)DE-He213 tetracycline (dpeaa)DE-He213 Schlünzen, Frank verfasserin aut Harms, Jörg verfasserin aut Zarivach, Raz verfasserin aut Glühmann, Marco verfasserin aut Avila, Horacio verfasserin aut Bashan, Anat verfasserin aut Bartels, Heike verfasserin aut Auerbach, Tamar verfasserin aut Jacobi, Carsten verfasserin aut Hartsch, Thomas verfasserin aut Yonath, Ada verfasserin aut Franceschi, François verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 20(2001), 8 vom: 17. Apr., Seite 1829-1839 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:20 year:2001 number:8 day:17 month:04 pages:1829-1839 https://dx.doi.org/10.1093/emboj/20.8.1829 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 20 2001 8 17 04 1829-1839 |
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Enthalten in The EMBO Journal 20(2001), 8 vom: 17. Apr., Seite 1829-1839 volume:20 year:2001 number:8 day:17 month:04 pages:1829-1839 |
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Pioletti, Marta @@aut@@ Schlünzen, Frank @@aut@@ Harms, Jörg @@aut@@ Zarivach, Raz @@aut@@ Glühmann, Marco @@aut@@ Avila, Horacio @@aut@@ Bashan, Anat @@aut@@ Bartels, Heike @@aut@@ Auerbach, Tamar @@aut@@ Jacobi, Carsten @@aut@@ Hartsch, Thomas @@aut@@ Yonath, Ada @@aut@@ Franceschi, François @@aut@@ |
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We analyzed by X‐ray crystallography the structures of three different complexes of the small ribosomal subunit of Thermus thermophilus with the A‐site inhibitor tetracycline, the universal initiation inhibitor edeine and the C‐terminal domain of the translation initiation factor IF3. The crystal structure analysis of the complex with tetracycline revealed the functionally important site responsible for the blockage of the A‐site. Five additional tetracycline sites resolve most of the controversial biochemical data on the location of tetracycline. The interaction of edeine with the small subunit indicates its role in inhibiting initiation and shows its involvement with P‐site tRNA. 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Pioletti, Marta |
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Pioletti, Marta misc antibiotics misc edeine misc IF3 misc ribosomes misc tetracycline Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3 |
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Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3 antibiotics (dpeaa)DE-He213 edeine (dpeaa)DE-He213 IF3 (dpeaa)DE-He213 ribosomes (dpeaa)DE-He213 tetracycline (dpeaa)DE-He213 |
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Pioletti, Marta Schlünzen, Frank Harms, Jörg Zarivach, Raz Glühmann, Marco Avila, Horacio Bashan, Anat Bartels, Heike Auerbach, Tamar Jacobi, Carsten Hartsch, Thomas Yonath, Ada Franceschi, François |
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crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and if3 |
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Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3 |
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Abstract The small ribosomal subunit is responsible for the decoding of genetic information and plays a key role in the initiation of protein synthesis. We analyzed by X‐ray crystallography the structures of three different complexes of the small ribosomal subunit of Thermus thermophilus with the A‐site inhibitor tetracycline, the universal initiation inhibitor edeine and the C‐terminal domain of the translation initiation factor IF3. The crystal structure analysis of the complex with tetracycline revealed the functionally important site responsible for the blockage of the A‐site. Five additional tetracycline sites resolve most of the controversial biochemical data on the location of tetracycline. The interaction of edeine with the small subunit indicates its role in inhibiting initiation and shows its involvement with P‐site tRNA. The location of the C‐terminal domain of IF3, at the solvent side of the platform, sheds light on the formation of the initiation complex, and implies that the anti‐association activity of IF3 is due to its influence on the conformational dynamics of the small ribosomal subunit. © European Molecular Biology Organization 2001 |
| abstractGer |
Abstract The small ribosomal subunit is responsible for the decoding of genetic information and plays a key role in the initiation of protein synthesis. We analyzed by X‐ray crystallography the structures of three different complexes of the small ribosomal subunit of Thermus thermophilus with the A‐site inhibitor tetracycline, the universal initiation inhibitor edeine and the C‐terminal domain of the translation initiation factor IF3. The crystal structure analysis of the complex with tetracycline revealed the functionally important site responsible for the blockage of the A‐site. Five additional tetracycline sites resolve most of the controversial biochemical data on the location of tetracycline. The interaction of edeine with the small subunit indicates its role in inhibiting initiation and shows its involvement with P‐site tRNA. The location of the C‐terminal domain of IF3, at the solvent side of the platform, sheds light on the formation of the initiation complex, and implies that the anti‐association activity of IF3 is due to its influence on the conformational dynamics of the small ribosomal subunit. © European Molecular Biology Organization 2001 |
| abstract_unstemmed |
Abstract The small ribosomal subunit is responsible for the decoding of genetic information and plays a key role in the initiation of protein synthesis. We analyzed by X‐ray crystallography the structures of three different complexes of the small ribosomal subunit of Thermus thermophilus with the A‐site inhibitor tetracycline, the universal initiation inhibitor edeine and the C‐terminal domain of the translation initiation factor IF3. The crystal structure analysis of the complex with tetracycline revealed the functionally important site responsible for the blockage of the A‐site. Five additional tetracycline sites resolve most of the controversial biochemical data on the location of tetracycline. The interaction of edeine with the small subunit indicates its role in inhibiting initiation and shows its involvement with P‐site tRNA. The location of the C‐terminal domain of IF3, at the solvent side of the platform, sheds light on the formation of the initiation complex, and implies that the anti‐association activity of IF3 is due to its influence on the conformational dynamics of the small ribosomal subunit. © European Molecular Biology Organization 2001 |
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Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3 |
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Schlünzen, Frank Harms, Jörg Zarivach, Raz Glühmann, Marco Avila, Horacio Bashan, Anat Bartels, Heike Auerbach, Tamar Jacobi, Carsten Hartsch, Thomas Yonath, Ada Franceschi, François |
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Schlünzen, Frank Harms, Jörg Zarivach, Raz Glühmann, Marco Avila, Horacio Bashan, Anat Bartels, Heike Auerbach, Tamar Jacobi, Carsten Hartsch, Thomas Yonath, Ada Franceschi, François |
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|
| score |
7.399987 |