2v04

CRYSTAL STRUCTURE OF CHOLINE BINDING PROTEIN F FROM STREPTOCOCCUS PNEUMONIAE

spinqualitylabelsall models 2v04, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2v04 is a 1 chain structure with sequence from Strr6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CHT Related: 2v05 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Crystal structure of CbpF, a bifunctional choline-binding protein and autolysis regulator from Streptococcus pneumoniae.,Molina R, Gonzalez A, Stelter M, Perez-Dorado I, Kahn R, Morales M, Moscoso M, Campuzano S, Campillo NE, Mobashery S, Garcia JL, Garcia P, Hermoso JA EMBO Rep. 2009 Mar;10(3):246-51. Epub 2009 Jan 23. PMID:19165143 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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