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The three\u2010dimensional structure of choline\u2010binding 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\u2010consensus choline\u2010binding repeats, distributed along its length, which markedly alter its shape, charge distribution and binding ability, and organizing the protein into two well\u2010defined modules. The carboxy\u2010terminal module is involved in cell wall binding and the amino\u2010terminal module is crucial for inhibition of the autolytic LytC muramidase, providing a regulatory function for pneumococcal autolysis.<\/jats:p>","DOI":"10.1038\/embor.2008.245","type":"journal-article","created":{"date-parts":[[2009,1,23]],"date-time":"2009-01-23T07:39:29Z","timestamp":1232696369000},"page":"246-251","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":39,"title":["Crystal structure of CbpF, a bifunctional choline\u2010binding protein and autolysis regulator from\n                    <i>Streptococcus pneumoniae<\/i>"],"prefix":"10.1038","volume":"10","author":[{"given":"Rafael","family":"Molina","sequence":"first","affiliation":[{"name":"Grupo de Cristalografia Macromolecular y Biologia Estructural, Instituto Qu\u00edmica\u2010F\u00edsica Rocasolano, CSIC  Serrano 119 28006 Madrid Spain"}]},{"given":"Ana","family":"Gonz\u00e1lez","sequence":"additional","affiliation":[{"name":"Departamento de Microbiologia Molecular, Centro de Investigaciones Biol\u00f3gicas, CSIC, and Ciber de Enfermedades Respiratorias  Ramiro de Maeztu 9 28040 Madrid Spain"}]},{"given":"Meike","family":"Stelter","sequence":"additional","affiliation":[{"name":"Laboratoire de Cristallographie Macromol\u00e9culaire, Institut de Biologie Structurale J.\u2010P. 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