6rth

Crystal structure of the ligand-free glycosyltransferase domain from the YGT toxin

spinqualitylabelsall models 6rth, resolution 3.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6rth is a 2 chain structure with sequence from Yersinia mollaretii ATCC 43969. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.4Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed We identified a glucosyltransferase (YGT) and an ADP-ribosyltransferase (YART) in Yersinia mollaretii, highly related to glucosylating toxins from Clostridium difficile, the cause of antibiotics-associated enterocolitis. Both Yersinia toxins consist of an amino-terminal enzyme domain, an autoprotease domain activated by inositol hexakisphosphate, and a carboxyl-terminal translocation domain. YGT N-acetylglucosaminylates Rab5 and Rab31 at Thr(52) and Thr(36), respectively, thereby inactivating the Rab proteins. YART ADP-ribosylates Rab5 and Rab31 at Gln(79) and Gln(64), respectively. This activates Rab proteins by inhibiting GTP hydrolysis. We determined the crystal structure of the glycosyltransferase domain of YGT (YGT(G)) in the presence and absence of UDP at 1.9- and 3.4-A resolution, respectively. Thereby, we identified a previously unknown potassium ion-binding site, which explains potassium ion-dependent enhanced glycosyltransferase activity in clostridial and related toxins. Our findings exhibit a novel type of inverse regulation of Rab proteins by toxins and provide new insights into the structure-function relationship of glycosyltransferase toxins. Inverse control of Rab proteins by Yersinia ADP-ribosyltransferase and glycosyltransferase related to clostridial glucosylating toxins.,Ost GS, Wirth C, Bogdanovic X, Kao WC, Schorch B, Aktories PJK, Papatheodorou P, Schwan C, Schlosser A, Jank T, Hunte C, Aktories K Sci Adv. 2020 Mar 11;6(11):eaaz2094. doi: 10.1126/sciadv.aaz2094. eCollection, 2020 Mar. PMID:32195351 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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