2izp | pdb_00002izp

BipD - an invasion protein associated with the type-III secretion system of Burkholderia pseudomallei.

spinqualitylabelsall models 2izp, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2izp is a 2 chain structure with sequence from Burkholderia pseudomallei. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function BIPD_BURPS Required for invasion of epithelial cells, as well as for survival within host cells, escape from endocytic vesicles and subsequent actin-tail formation. Probably regulates the secretion of effectors BipB and BipC and their final integration into the target cell membrane. 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 Burkoldheria pseudomallei is a Gram-negative bacterium that possesses a protein secretion system similar to those found in Salmonella and Shigella. Recent work has indicated that the protein encoded by the BipD gene of B. pseudomallei is an important secreted virulence factor. BipD is similar in sequence to IpaD from Shigella and SipD from Salmonella and is therefore likely to be a translocator protein in the type-III secretion system of B. pseudomallei. The crystal structure of BipD has been solved at a resolution of 2.1 A revealing the detailed tertiary fold of the molecule. The overall structure is appreciably extended and consists of a bundle of antiparallel alpha-helical segments with two small beta-sheet regions. The longest helices of the molecule form a four-helix bundle and most of the remaining secondary structure elements (three helices and two three-stranded beta-sheets) are formed by the region linking the last two helices of the four-helix bundle. The structure suggests that the biologically active form of the molecule may be a dimer formed by contacts involving the C-terminal alpha-helix, which is the most strongly conserved part of the protein. Comparison of the structure of BipD with immunological and other data for IpaD indicates that the C-terminal alpha-helix is also involved in contacts with other proteins that form the translocon. High resolution structure of BipD: an invasion protein associated with the type III secretion system of Burkholderia pseudomallei.,Erskine PT, Knight MJ, Ruaux A, Mikolajek H, Wong Fat Sang N, Withers J, Gill R, Wood SP, Wood M, Fox GC, Cooper JB J Mol Biol. 2006 Oct 13;363(1):125-36. Epub 2006 Aug 1. PMID:16950399 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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