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Title: | Crystal structure of CbpF, a bifunctional choline-binding protein and autolysis regulator from Streptococcus pneumoniae |
Authors: | Molina, Rafael; González, Ana ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() |
Keywords: | CBP family Crystallography Pneumococcus CbpF Virulence |
Issue Date: | 23-Jan-2009 |
Publisher: | Nature Publishing Group |
Citation: | EMBO Reports, doi: 10.1038/embor.2008.245 |
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. |
Description: | 6 pages, 5 figures.-- PMID: 19165143 [PubMed]. |
Publisher version (URL): | 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 |
Appears in Collections: | (IQM) Artículos (IQFR) Artículos (CIB) Artículos |
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