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Título : Crystal structure of CbpF, a bifunctional choline-binding protein and autolysis regulator from Streptococcus pneumoniae
Autor : 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.
Palabras clave : CBP family
Fecha de publicación : 23-Jan-2009
Editor: Nature Publishing Group
Resumen: 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.
Descripción : 6 pages, 5 figures.-- PMID: 19165143 [PubMed].
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ISSN: 1469-221X
DOI: 10.1038/embor.2008.245
Citación : EMBO Reports, doi: 10.1038/embor.2008.245
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