Journal
EMBO REPORTS
Volume 10, Issue 3, Pages 246-251Publisher
WILEY
DOI: 10.1038/embor.2008.245
Keywords
CBP family; crystallography; pneumococcus; CbpF; virulence
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Funding
- Spanish Ministry of Science and Technology [BFU2005-01645, SAF2006-00390]
- COMBACT [S-BIO-0260/2006]
- CIBER de Enfermedades Respiratorias (CIBERES)
- National Institutes of Health
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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.
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