1dm0 | pdb_00001dm0

SHIGA TOXIN

spinqualitylabelsall models 1dm0, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1dm0 is a 12 chain structure with sequence from "bacillus_dysenteriae"_shiga_1898 "bacillus dysenteriae" shiga 1898. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Activity: rRNA N-glycosylase, with EC number 3.2.2.22 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [STXB_SHIDY] The B subunit is responsible for the binding of the holotoxin to specific receptors on the target cell surface, such as globotriaosylceramide (Gb3) in human intestinal microvilli. 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 Shigella dysenteriae is the pathogen responsible for the severe form of dysentery in humans. It produces Shiga toxin, the prototype of a family of closely related bacterial protein toxins. We have determined the structure of the holotoxin, an AB5 hexamer, by X-ray crystallography. The five B subunits form a pentameric ring, encircling a helix at the carboxy terminus of the A subunit. The A subunit interacts with the B pentamer via this C-terminal helix and a four-stranded mixed beta-sheet. The fold of the rest of the A subunit is similar to that of the A chain of the plant toxin ricin; both are N-glycosidases. However, the active site in the bacterial holotoxin is blocked by a segment of polypeptide chain. These residues of the A subunit would be released as part of the activation mechanism of the toxin. Crystal structure of the holotoxin from Shigella dysenteriae at 2.5 A resolution.,Fraser ME, Chernaia MM, Kozlov YV, James MN Nat Struct Biol. 1994 Jan;1(1):59-64. PMID:7656009 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Shiga toxin

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