Crystal structure of CbpF, a bifunctional choline‐binding protein and autolysis regulator from Streptococcus pneumoniae
Abstract Phosphorylcholine, a crucial component of the pneumococcal cell wall, is essential in bacterial physiology and in human pathogenesis because it binds to serum components of the immune system and acts as a docking station for the family of surface choline‐binding proteins. The three‐dimensio...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Molina, Rafael [verfasserIn] González, Ana [verfasserIn] Stelter, Meike [verfasserIn] Pérez‐Dorado, Inmaculada [verfasserIn] Kahn, Richard [verfasserIn] Morales, María [verfasserIn] Campuzano, Susana [verfasserIn] Campillo, Nuria E [verfasserIn] Mobashery, Shahriar [verfasserIn] García, José L [verfasserIn] García, Pedro [verfasserIn] Hermoso, Juan A [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2009 |
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| Schlagwörter: |
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| Anmerkung: |
© European Molecular Biology Organization 2009 |
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| Übergeordnetes Werk: |
Enthalten in: EMBO Reports - Nature Publishing Group UK, 2023, 10(2009), 3 vom: 23. Jan., Seite 246-251 |
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| Übergeordnetes Werk: |
volume:10 ; year:2009 ; number:3 ; day:23 ; month:01 ; pages:246-251 |
| Links: |
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| DOI / URN: |
10.1038/embor.2008.245 |
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| Katalog-ID: |
SPR058080856 |
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| 100 | 1 | |a Molina, Rafael |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Crystal structure of CbpF, a bifunctional choline‐binding protein and autolysis regulator from Streptococcus pneumoniae |
| 264 | 1 | |c 2009 | |
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| 520 | |a Abstract Phosphorylcholine, a crucial component of the pneumococcal cell wall, is essential in bacterial physiology and in human pathogenesis because it binds to serum components of the immune system and acts as a docking station for the family of surface choline‐binding proteins. The three‐dimensional structure of choline‐binding protein F (CbpF), one of the most abundant proteins in the pneumococcal cell wall, has been solved in complex with choline. CbpF shows a new modular structure composed both of consensus and non‐consensus choline‐binding repeats, distributed along its length, which markedly alter its shape, charge distribution and binding ability, and organizing the protein into two well‐defined modules. The carboxy‐terminal module is involved in cell wall binding and the amino‐terminal module is crucial for inhibition of the autolytic LytC muramidase, providing a regulatory function for pneumococcal autolysis. | ||
| 650 | 4 | |a CBP family |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a crystallography |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a pneumococcus |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a CbpF |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a virulence |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a González, Ana |e verfasserin |4 aut | |
| 700 | 1 | |a Stelter, Meike |e verfasserin |4 aut | |
| 700 | 1 | |a Pérez‐Dorado, Inmaculada |e verfasserin |4 aut | |
| 700 | 1 | |a Kahn, Richard |e verfasserin |4 aut | |
| 700 | 1 | |a Morales, María |e verfasserin |4 aut | |
| 700 | 1 | |a Campuzano, Susana |e verfasserin |4 aut | |
| 700 | 1 | |a Campillo, Nuria E |e verfasserin |4 aut | |
| 700 | 1 | |a Mobashery, Shahriar |e verfasserin |4 aut | |
| 700 | 1 | |a García, José L |e verfasserin |4 aut | |
| 700 | 1 | |a García, Pedro |e verfasserin |4 aut | |
| 700 | 1 | |a Hermoso, Juan A |e verfasserin |4 aut | |
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10.1038/embor.2008.245 doi (DE-627)SPR058080856 (SPR)embor.2008.245-e DE-627 ger DE-627 rakwb eng Molina, Rafael verfasserin aut Crystal structure of CbpF, a bifunctional choline‐binding protein and autolysis regulator from Streptococcus pneumoniae 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2009 Abstract Phosphorylcholine, a crucial component of the pneumococcal cell wall, is essential in bacterial physiology and in human pathogenesis because it binds to serum components of the immune system and acts as a docking station for the family of surface choline‐binding proteins. The three‐dimensional structure of choline‐binding protein F (CbpF), one of the most abundant proteins in the pneumococcal cell wall, has been solved in complex with choline. CbpF shows a new modular structure composed both of consensus and non‐consensus choline‐binding repeats, distributed along its length, which markedly alter its shape, charge distribution and binding ability, and organizing the protein into two well‐defined modules. The carboxy‐terminal module is involved in cell wall binding and the amino‐terminal module is crucial for inhibition of the autolytic LytC muramidase, providing a regulatory function for pneumococcal autolysis. CBP family (dpeaa)DE-He213 crystallography (dpeaa)DE-He213 pneumococcus (dpeaa)DE-He213 CbpF (dpeaa)DE-He213 virulence (dpeaa)DE-He213 González, Ana verfasserin aut Stelter, Meike verfasserin aut Pérez‐Dorado, Inmaculada verfasserin aut Kahn, Richard verfasserin aut Morales, María verfasserin aut Campuzano, Susana verfasserin aut Campillo, Nuria E verfasserin aut Mobashery, Shahriar verfasserin aut García, José L verfasserin aut García, Pedro verfasserin aut Hermoso, Juan A verfasserin aut Enthalten in EMBO Reports Nature Publishing Group UK, 2023 10(2009), 3 vom: 23. Jan., Seite 246-251 (DE-627)320645622 (DE-600)2025376-X 1469-3178 nnns volume:10 year:2009 number:3 day:23 month:01 pages:246-251 https://dx.doi.org/10.1038/embor.2008.245 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_11 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_60 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_370 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 10 2009 3 23 01 246-251 |
| spelling |
10.1038/embor.2008.245 doi (DE-627)SPR058080856 (SPR)embor.2008.245-e DE-627 ger DE-627 rakwb eng Molina, Rafael verfasserin aut Crystal structure of CbpF, a bifunctional choline‐binding protein and autolysis regulator from Streptococcus pneumoniae 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2009 Abstract Phosphorylcholine, a crucial component of the pneumococcal cell wall, is essential in bacterial physiology and in human pathogenesis because it binds to serum components of the immune system and acts as a docking station for the family of surface choline‐binding proteins. The three‐dimensional structure of choline‐binding protein F (CbpF), one of the most abundant proteins in the pneumococcal cell wall, has been solved in complex with choline. CbpF shows a new modular structure composed both of consensus and non‐consensus choline‐binding repeats, distributed along its length, which markedly alter its shape, charge distribution and binding ability, and organizing the protein into two well‐defined modules. The carboxy‐terminal module is involved in cell wall binding and the amino‐terminal module is crucial for inhibition of the autolytic LytC muramidase, providing a regulatory function for pneumococcal autolysis. CBP family (dpeaa)DE-He213 crystallography (dpeaa)DE-He213 pneumococcus (dpeaa)DE-He213 CbpF (dpeaa)DE-He213 virulence (dpeaa)DE-He213 González, Ana verfasserin aut Stelter, Meike verfasserin aut Pérez‐Dorado, Inmaculada verfasserin aut Kahn, Richard verfasserin aut Morales, María verfasserin aut Campuzano, Susana verfasserin aut Campillo, Nuria E verfasserin aut Mobashery, Shahriar verfasserin aut García, José L verfasserin aut García, Pedro verfasserin aut Hermoso, Juan A verfasserin aut Enthalten in EMBO Reports Nature Publishing Group UK, 2023 10(2009), 3 vom: 23. Jan., Seite 246-251 (DE-627)320645622 (DE-600)2025376-X 1469-3178 nnns volume:10 year:2009 number:3 day:23 month:01 pages:246-251 https://dx.doi.org/10.1038/embor.2008.245 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_11 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_60 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_370 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 10 2009 3 23 01 246-251 |
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10.1038/embor.2008.245 doi (DE-627)SPR058080856 (SPR)embor.2008.245-e DE-627 ger DE-627 rakwb eng Molina, Rafael verfasserin aut Crystal structure of CbpF, a bifunctional choline‐binding protein and autolysis regulator from Streptococcus pneumoniae 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2009 Abstract Phosphorylcholine, a crucial component of the pneumococcal cell wall, is essential in bacterial physiology and in human pathogenesis because it binds to serum components of the immune system and acts as a docking station for the family of surface choline‐binding proteins. The three‐dimensional structure of choline‐binding protein F (CbpF), one of the most abundant proteins in the pneumococcal cell wall, has been solved in complex with choline. CbpF shows a new modular structure composed both of consensus and non‐consensus choline‐binding repeats, distributed along its length, which markedly alter its shape, charge distribution and binding ability, and organizing the protein into two well‐defined modules. The carboxy‐terminal module is involved in cell wall binding and the amino‐terminal module is crucial for inhibition of the autolytic LytC muramidase, providing a regulatory function for pneumococcal autolysis. CBP family (dpeaa)DE-He213 crystallography (dpeaa)DE-He213 pneumococcus (dpeaa)DE-He213 CbpF (dpeaa)DE-He213 virulence (dpeaa)DE-He213 González, Ana verfasserin aut Stelter, Meike verfasserin aut Pérez‐Dorado, Inmaculada verfasserin aut Kahn, Richard verfasserin aut Morales, María verfasserin aut Campuzano, Susana verfasserin aut Campillo, Nuria E verfasserin aut Mobashery, Shahriar verfasserin aut García, José L verfasserin aut García, Pedro verfasserin aut Hermoso, Juan A verfasserin aut Enthalten in EMBO Reports Nature Publishing Group UK, 2023 10(2009), 3 vom: 23. Jan., Seite 246-251 (DE-627)320645622 (DE-600)2025376-X 1469-3178 nnns volume:10 year:2009 number:3 day:23 month:01 pages:246-251 https://dx.doi.org/10.1038/embor.2008.245 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_11 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_60 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_370 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 10 2009 3 23 01 246-251 |
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10.1038/embor.2008.245 doi (DE-627)SPR058080856 (SPR)embor.2008.245-e DE-627 ger DE-627 rakwb eng Molina, Rafael verfasserin aut Crystal structure of CbpF, a bifunctional choline‐binding protein and autolysis regulator from Streptococcus pneumoniae 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2009 Abstract Phosphorylcholine, a crucial component of the pneumococcal cell wall, is essential in bacterial physiology and in human pathogenesis because it binds to serum components of the immune system and acts as a docking station for the family of surface choline‐binding proteins. The three‐dimensional structure of choline‐binding protein F (CbpF), one of the most abundant proteins in the pneumococcal cell wall, has been solved in complex with choline. CbpF shows a new modular structure composed both of consensus and non‐consensus choline‐binding repeats, distributed along its length, which markedly alter its shape, charge distribution and binding ability, and organizing the protein into two well‐defined modules. The carboxy‐terminal module is involved in cell wall binding and the amino‐terminal module is crucial for inhibition of the autolytic LytC muramidase, providing a regulatory function for pneumococcal autolysis. CBP family (dpeaa)DE-He213 crystallography (dpeaa)DE-He213 pneumococcus (dpeaa)DE-He213 CbpF (dpeaa)DE-He213 virulence (dpeaa)DE-He213 González, Ana verfasserin aut Stelter, Meike verfasserin aut Pérez‐Dorado, Inmaculada verfasserin aut Kahn, Richard verfasserin aut Morales, María verfasserin aut Campuzano, Susana verfasserin aut Campillo, Nuria E verfasserin aut Mobashery, Shahriar verfasserin aut García, José L verfasserin aut García, Pedro verfasserin aut Hermoso, Juan A verfasserin aut Enthalten in EMBO Reports Nature Publishing Group UK, 2023 10(2009), 3 vom: 23. Jan., Seite 246-251 (DE-627)320645622 (DE-600)2025376-X 1469-3178 nnns volume:10 year:2009 number:3 day:23 month:01 pages:246-251 https://dx.doi.org/10.1038/embor.2008.245 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_11 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_60 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_370 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 10 2009 3 23 01 246-251 |
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10.1038/embor.2008.245 doi (DE-627)SPR058080856 (SPR)embor.2008.245-e DE-627 ger DE-627 rakwb eng Molina, Rafael verfasserin aut Crystal structure of CbpF, a bifunctional choline‐binding protein and autolysis regulator from Streptococcus pneumoniae 2009 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2009 Abstract Phosphorylcholine, a crucial component of the pneumococcal cell wall, is essential in bacterial physiology and in human pathogenesis because it binds to serum components of the immune system and acts as a docking station for the family of surface choline‐binding proteins. The three‐dimensional structure of choline‐binding protein F (CbpF), one of the most abundant proteins in the pneumococcal cell wall, has been solved in complex with choline. CbpF shows a new modular structure composed both of consensus and non‐consensus choline‐binding repeats, distributed along its length, which markedly alter its shape, charge distribution and binding ability, and organizing the protein into two well‐defined modules. The carboxy‐terminal module is involved in cell wall binding and the amino‐terminal module is crucial for inhibition of the autolytic LytC muramidase, providing a regulatory function for pneumococcal autolysis. CBP family (dpeaa)DE-He213 crystallography (dpeaa)DE-He213 pneumococcus (dpeaa)DE-He213 CbpF (dpeaa)DE-He213 virulence (dpeaa)DE-He213 González, Ana verfasserin aut Stelter, Meike verfasserin aut Pérez‐Dorado, Inmaculada verfasserin aut Kahn, Richard verfasserin aut Morales, María verfasserin aut Campuzano, Susana verfasserin aut Campillo, Nuria E verfasserin aut Mobashery, Shahriar verfasserin aut García, José L verfasserin aut García, Pedro verfasserin aut Hermoso, Juan A verfasserin aut Enthalten in EMBO Reports Nature Publishing Group UK, 2023 10(2009), 3 vom: 23. Jan., Seite 246-251 (DE-627)320645622 (DE-600)2025376-X 1469-3178 nnns volume:10 year:2009 number:3 day:23 month:01 pages:246-251 https://dx.doi.org/10.1038/embor.2008.245 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_11 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_60 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_370 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 10 2009 3 23 01 246-251 |
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Enthalten in EMBO Reports 10(2009), 3 vom: 23. Jan., Seite 246-251 volume:10 year:2009 number:3 day:23 month:01 pages:246-251 |
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Molina, Rafael @@aut@@ González, Ana @@aut@@ Stelter, Meike @@aut@@ Pérez‐Dorado, Inmaculada @@aut@@ Kahn, Richard @@aut@@ Morales, María @@aut@@ Campuzano, Susana @@aut@@ Campillo, Nuria E @@aut@@ Mobashery, Shahriar @@aut@@ García, José L @@aut@@ García, Pedro @@aut@@ Hermoso, Juan A @@aut@@ |
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Molina, Rafael |
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Molina, Rafael misc CBP family misc crystallography misc pneumococcus misc CbpF misc virulence Crystal structure of CbpF, a bifunctional choline‐binding protein and autolysis regulator from Streptococcus pneumoniae |
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Crystal structure of CbpF, a bifunctional choline‐binding protein and autolysis regulator from Streptococcus pneumoniae CBP family (dpeaa)DE-He213 crystallography (dpeaa)DE-He213 pneumococcus (dpeaa)DE-He213 CbpF (dpeaa)DE-He213 virulence (dpeaa)DE-He213 |
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Molina, Rafael González, Ana Stelter, Meike Pérez‐Dorado, Inmaculada Kahn, Richard Morales, María Campuzano, Susana Campillo, Nuria E Mobashery, Shahriar García, José L García, Pedro Hermoso, Juan A |
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Molina, Rafael |
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crystal structure of cbpf, a bifunctional choline‐binding protein and autolysis regulator from streptococcus pneumoniae |
| title_auth |
Crystal structure of CbpF, a bifunctional choline‐binding protein and autolysis regulator from Streptococcus pneumoniae |
| abstract |
Abstract Phosphorylcholine, a crucial component of the pneumococcal cell wall, is essential in bacterial physiology and in human pathogenesis because it binds to serum components of the immune system and acts as a docking station for the family of surface choline‐binding proteins. The three‐dimensional structure of choline‐binding protein F (CbpF), one of the most abundant proteins in the pneumococcal cell wall, has been solved in complex with choline. CbpF shows a new modular structure composed both of consensus and non‐consensus choline‐binding repeats, distributed along its length, which markedly alter its shape, charge distribution and binding ability, and organizing the protein into two well‐defined modules. The carboxy‐terminal module is involved in cell wall binding and the amino‐terminal module is crucial for inhibition of the autolytic LytC muramidase, providing a regulatory function for pneumococcal autolysis. © European Molecular Biology Organization 2009 |
| abstractGer |
Abstract Phosphorylcholine, a crucial component of the pneumococcal cell wall, is essential in bacterial physiology and in human pathogenesis because it binds to serum components of the immune system and acts as a docking station for the family of surface choline‐binding proteins. The three‐dimensional structure of choline‐binding protein F (CbpF), one of the most abundant proteins in the pneumococcal cell wall, has been solved in complex with choline. CbpF shows a new modular structure composed both of consensus and non‐consensus choline‐binding repeats, distributed along its length, which markedly alter its shape, charge distribution and binding ability, and organizing the protein into two well‐defined modules. The carboxy‐terminal module is involved in cell wall binding and the amino‐terminal module is crucial for inhibition of the autolytic LytC muramidase, providing a regulatory function for pneumococcal autolysis. © European Molecular Biology Organization 2009 |
| abstract_unstemmed |
Abstract Phosphorylcholine, a crucial component of the pneumococcal cell wall, is essential in bacterial physiology and in human pathogenesis because it binds to serum components of the immune system and acts as a docking station for the family of surface choline‐binding proteins. The three‐dimensional structure of choline‐binding protein F (CbpF), one of the most abundant proteins in the pneumococcal cell wall, has been solved in complex with choline. CbpF shows a new modular structure composed both of consensus and non‐consensus choline‐binding repeats, distributed along its length, which markedly alter its shape, charge distribution and binding ability, and organizing the protein into two well‐defined modules. The carboxy‐terminal module is involved in cell wall binding and the amino‐terminal module is crucial for inhibition of the autolytic LytC muramidase, providing a regulatory function for pneumococcal autolysis. © European Molecular Biology Organization 2009 |
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Crystal structure of CbpF, a bifunctional choline‐binding protein and autolysis regulator from Streptococcus pneumoniae |
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| score |
7.4010687 |