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dc.contributor.authorMolina, Rafael-
dc.contributor.authorGonzález, Ana-
dc.contributor.authorStelter, Meike-
dc.contributor.authorPérez-Dorado, Inmaculada-
dc.contributor.authorKahn, Richard-
dc.contributor.authorMorales, María-
dc.contributor.authorCampuzano, Susana-
dc.contributor.authorCampillo, Nuria E.-
dc.contributor.authorMobashery, Shahriar-
dc.contributor.authorGarcía, José Luis-
dc.contributor.authorGarcía, Pedro-
dc.contributor.authorHermoso, Juan A.-
dc.identifier.citationEMBO Reports, doi: 10.1038/embor.2008.245en_US
dc.description6 pages, 5 figures.-- PMID: 19165143 [PubMed].en_US
dc.description.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.en_US
dc.description.sponsorshipThis study was supported by grants from the Spanish Ministry of Science and Technology (BFU2005-01645 and SAF2006-00390) and by the COMBACT program of the Comunidad de Madrid (S-BIO-0260/2006) and CIBER de Enfermedades Respiratorias (CIBERES), which is an initiative of Spanish Instituto de Salud Carlos III. R.M. and A.G. hold a fellowship from the Spanish Ministry of Science and Technology. S.C. holds a Juan de la Cierva fellowship from the Spanish Ministry of Science and Technology. The study in the USA was supported by the National Institutes of Health.en_US
dc.format.extent811144 bytes-
dc.publisherNature Publishing Groupen_US
dc.subjectCBP familyen_US
dc.titleCrystal structure of CbpF, a bifunctional choline-binding protein and autolysis regulator from Streptococcus pneumoniaeen_US
dc.description.peerreviewedPeer revieweden_US
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