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Título: | Crystal structure of CbpF, a bifunctional choline-binding protein and autolysis regulator from Streptococcus pneumoniae |
Autor: | Molina, Rafael CSIC ORCID; González, Ana CSIC; Stelter, Meike; Pérez-Dorado, Inmaculada CSIC ORCID; Kahn, Richard; Morales, María CSIC; Campuzano, Susana CSIC ORCID; Campillo, Nuria E. CSIC ORCID ; Mobashery, Shahriar; García, José Luis CSIC ORCID ; García, Pedro CSIC ORCID ; Hermoso, Juan A. CSIC ORCID | Palabras clave: | CBP family Crystallography Pneumococcus CbpF Virulence |
Fecha de publicación: | 23-ene-2009 | Editor: | Nature Publishing Group | Citación: | EMBO Reports, doi: 10.1038/embor.2008.245 | Resumen: | 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. | Descripción: | 6 pages, 5 figures.-- PMID: 19165143 [PubMed]. | Versión del editor: | http://dx.doi.org/10.1038/embor.2008.245 | URI: | http://hdl.handle.net/10261/10646 | DOI: | 10.1038/embor.2008.245 | ISSN: | 1469-221X |
Aparece en las colecciones: | (IQM) Artículos (IQF) Artículos (CIB) Artículos |
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