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Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/10646
Title: 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, José Luis; García, Pedro; Hermoso, Juan A.
Keywords: CBP family
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
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