title: Crystal structure of CbpF, a bifunctional choline-binding protein and autolysis regulator from Streptococcus pneumoniae.
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.
authors.affiliation: Grupo de Cristalografia Macromolecular y Biologia Estructural, Instituto Química-Física Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain.
authors.forename: Rafael
authors.initials: R
authors.lastname: Molina
authors.forename: Ana
authors.initials: A
authors.lastname: González
authors.forename: Meike
authors.initials: M
authors.lastname: Stelter
authors.forename: Inmaculada
authors.initials: I
authors.lastname: Pérez-Dorado
authors.forename: Richard
authors.initials: R
authors.lastname: Kahn
authors.forename: María
authors.initials: M
authors.lastname: Morales
authors.forename: Miriam
authors.initials: M
authors.lastname: Moscoso
authors.forename: Susana
authors.initials: S
authors.lastname: Campuzano
authors.forename: Nuria E
authors.initials: NE
authors.lastname: Campillo
authors.forename: Shahriar
authors.initials: S
authors.lastname: Mobashery
authors.forename: José L
authors.initials: JL
authors.lastname: García
authors.forename: Pedro
authors.initials: P
authors.lastname: García
authors.forename: Juan A
authors.initials: JA
authors.lastname: Hermoso
mesh_terms: D000595:Amino Acid Sequence; D001329:Autolysis; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D002794:Choline / Q000378:metabolism*; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000378:metabolism; D010457:Peptidoglycan / Q000378:metabolism; D017434:Protein Structure, Tertiary; D011956:Receptors, Cell Surface / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D013296:Streptococcus pneumoniae / Q000235:genetics / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D010457:Peptidoglycan; D011956:Receptors, Cell Surface; C419222:LytC protein, Streptococcus; D009238:N-Acetylmuramoyl-L-alanine Amidase; D002794:Choline