3kpt | pdb_00003kpt

Crystal structure of BcpA, the major pilin subunit of Bacillus cereus

spinqualitylabelsall models 3kpt, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3kpt is a 2 chain structure with sequence from Baccr. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA NonStd Res: MSE Gene: bcpA, BC_2508 (BACCR) 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 Gram-positive bacteria elaborate pili and do so without the participation of folding chaperones or disulfide bond catalysts. Sortases, enzymes that cut pilin precursors, form covalent bonds that link pilin subunits and assemble pili on the bacterial surface. We determined the x-ray structure of BcpA, the major pilin subunit of Bacillus cereus. The BcpA precursor encompasses 2 Ig folds (CNA(2) and CNA(3)) and one jelly-roll domain (XNA) each of which synthesizes a single intramolecular amide bond. A fourth amide bond, derived from the Ig fold of CNA(1), is formed only after pilin subunits have been incorporated into pili. We report that the domains of pilin precursors have evolved to synthesize a discrete sequence of intramolecular amide bonds, thereby conferring structural stability and protease resistance to pili. Intramolecular amide bonds stabilize pili on the surface of bacilli.,Budzik JM, Poor CB, Faull KF, Whitelegge JP, He C, Schneewind O Proc Natl Acad Sci U S A. 2009 Nov 10. PMID:19903875 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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