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Closed Access item Crystal structure of CbpF, a bifunctional choline-binding protein and autolysis regulator from Streptococcus pneumoniae

Authors:Molina, Rafael
González, Ana
Stelter, Meike
Pérez-Dorado, Inmaculada
Kahn, Richard
Morales, María
Campuzano, Susana
Campillo, Nuria Eugenia
Mobashery, Shahriar
García López, José Luis
García, Pedro
Hermoso, Juan A.
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
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