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Título

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

AutorMolina, 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.
Palabras claveCBP family
Crystallography
Pneumococcus
CbpF
Virulence
Fecha de publicación23-ene-2009
EditorNature Publishing Group
CitaciónEMBO Reports, doi: 10.1038/embor.2008.245
ResumenPhosphorylcholine, 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.
Descripción6 pages, 5 figures.-- PMID: 19165143 [PubMed].
Versión del editorhttp://dx.doi.org/10.1038/embor.2008.245
URIhttp://hdl.handle.net/10261/10646
DOI10.1038/embor.2008.245
ISSN1469-221X
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