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Crystal structure of CbpF, a bifunctional choline‐binding protein and autolysis regulator from Streptococcus pneumoniae
Author(s) -
Molina Rafael,
González Ana,
Stelter Meike,
PérezDorado Inmaculada,
Kahn Richard,
Morales María,
Campuzano Susana,
Campillo Nuria E,
Mobashery Shahriar,
García José L,
García Pedro,
Hermoso Juan A
Publication year - 2009
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/embor.2008.245
Subject(s) - autolysis (biology) , phosphorylcholine , choline , biology , biochemistry , binding protein , microbiology and biotechnology , chemistry , enzyme , gene
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.