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

AuthorsMolina, Rafael; González, Ana ; Stelter, Meike; Pérez-Dorado, Inmaculada ; Kahn, Richard; Morales, María ; Campuzano, Susana ; Campillo, Nuria E. ; Mobashery, Shahriar; García, José Luis ; García, Pedro ; Hermoso, Juan A.
KeywordsCBP family
Issue Date23-Jan-2009
PublisherNature Publishing Group
CitationEMBO Reports, doi: 10.1038/embor.2008.245
AbstractPhosphorylcholine, 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.
Description6 pages, 5 figures.-- PMID: 19165143 [PubMed].
Publisher version (URL)http://dx.doi.org/10.1038/embor.2008.245
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