Crystal structure of CbpF,a bifunctional choline‐binding protein and autolysis regulator from Streptococcus pneumoniae |
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| Authors: | Meike Stelter Inmaculada Pérez‐Dorado Richard Kahn María Morales Susana Campuzano Nuria E Campillo Shahriar Mobashery José L García Pedro García Juan A Hermoso |
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| Affiliation: | 1. Laboratoire de Cristallographie Macromoléculaire, Institut de Biologie Structurale J.‐P. Ebel CEA‐CNRS‐UJF, 41 rue Jules Horowitz, 38027 Grenoble Cedex 1, France;2. Grupo de Cristalografia Macromolecular y Biologia Estructural, Instituto Química‐Física Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain;3. Departamento de Microbiologia Molecular, Centro de Investigaciones Biológicas, CSIC, and Ciber de Enfermedades Respiratorias, Ramiro de Maeztu 9, 28040 Madrid, Spain;4. Departamento de Quimioterapia, Instituto de Química Médica, CSIC, Juan de la Cierva 3, 28006 Madrid, Spain;5. Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, Indiana, 46556 USA |
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| 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. |
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| Keywords: | CBP family crystallography pneumococcus CbpF virulence |
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