3b8p

Fragment of WzzB, Polysaccharide Co-polymerase from Salmonella Typhimurium

spinqualitylabelsall models 3b8p, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3b8p is a 5 chain structure with sequence from Salmonella enterica subsp. enterica serovar Typhimurium str. LT2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.1Å Ligands: MSE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN Function WZZB_SALTY Confers a modal distribution of chain length on the O-antigen component of lipopolysaccharide (LPS). Gives rise to a reduced number of short chain molecules and increases in numbers of longer molecules, with a modal value of 20. 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 The chain length distribution of complex polysaccharides present on the bacterial surface is determined by polysaccharide co-polymerases (PCPs) anchored in the inner membrane. We report crystal structures of the periplasmic domains of three PCPs that impart substantially different chain length distributions to surface polysaccharides. Despite very low sequence similarities, they have a common protomer structure with a long central alpha-helix extending 100 A into the periplasm. The protomers self-assemble into bell-shaped oligomers of variable sizes, with a large internal cavity. Electron microscopy shows that one of the full-length PCPs has a similar organization as that observed in the crystal for its periplasmic domain alone. Functional studies suggest that the top of the PCP oligomers is an important region for determining polysaccharide modal length. These structures provide a detailed view of components of the bacterial polysaccharide assembly machinery. Bacterial polysaccharide co-polymerases share a common framework for control of polymer length.,Tocilj A, Munger C, Proteau A, Morona R, Purins L, Ajamian E, Wagner J, Papadopoulos M, Van Den Bosch L, Rubinstein JL, Fethiere J, Matte A, Cygler M Nat Struct Mol Biol. 2008 Feb;15(2):130-8. Epub 2008 Jan 20. PMID:18204465 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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