6RTG
Crystal structure of the UDP-bound glycosyltransferase domain from the YGT toxin
6RTG の概要
| エントリーDOI | 10.2210/pdb6rtg/pdb |
| 分子名称 | RTX toxin and Ca2+-binding protein, URIDINE-5'-DIPHOSPHATE, MANGANESE (II) ION, ... (6 entities in total) |
| 機能のキーワード | glycosyltransferase domain, toxin, nucleotide binding |
| 由来する生物種 | Yersinia mollaretii (strain ATCC 43969 / DSM 18520 / CIP 103324 / CNY 7263 / WAIP 204) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 60648.52 |
| 構造登録者 | |
| 主引用文献 | Ost, G.S.,Wirth, C.,Bogdanovic, X.,Kao, W.C.,Schorch, B.,Aktories, P.J.K.,Papatheodorou, P.,Schwan, C.,Schlosser, A.,Jank, T.,Hunte, C.,Aktories, K. Inverse control of Rab proteins byYersiniaADP-ribosyltransferase and glycosyltransferase related to clostridial glucosylating toxins. Sci Adv, 6:eaaz2094-eaaz2094, 2020 Cited by PubMed Abstract: We identified a glucosyltransferase (YGT) and an ADP-ribosyltransferase (YART) in , highly related to glucosylating toxins from , the cause of antibiotics-associated enterocolitis. Both toxins consist of an amino-terminal enzyme domain, an autoprotease domain activated by inositol hexakisphosphate, and a carboxyl-terminal translocation domain. YGT -acetylglucosaminylates Rab5 and Rab31 at Thr and Thr, respectively, thereby inactivating the Rab proteins. YART ADP-ribosylates Rab5 and Rab31 at Gln and Gln, respectively. This activates Rab proteins by inhibiting GTP hydrolysis. We determined the crystal structure of the glycosyltransferase domain of YGT (YGT) in the presence and absence of UDP at 1.9- and 3.4-Å 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. PubMed: 32195351DOI: 10.1126/sciadv.aaz2094 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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