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-Structure paper
タイトル | A structural mechanism for bacterial autotransporter glycosylation by a dodecameric heptosyltransferase family. |
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ジャーナル・号・ページ | Elife, Vol. 3, Year 2014 |
掲載日 | 2014年10月13日 |
著者 | Qing Yao / Qiuhe Lu / Xiaobo Wan / Feng Song / Yue Xu / Mo Hu / Alla Zamyatina / Xiaoyun Liu / Niu Huang / Ping Zhu / Feng Shao / |
PubMed 要旨 | A large group of bacterial virulence autotransporters including AIDA-I from diffusely adhering E. coli (DAEC) and TibA from enterotoxigenic E. coli (ETEC) require hyperglycosylation for functioning. ...A large group of bacterial virulence autotransporters including AIDA-I from diffusely adhering E. coli (DAEC) and TibA from enterotoxigenic E. coli (ETEC) require hyperglycosylation for functioning. Here we demonstrate that TibC from ETEC harbors a heptosyltransferase activity on TibA and AIDA-I, defining a large family of bacterial autotransporter heptosyltransferases (BAHTs). The crystal structure of TibC reveals a characteristic ring-shape dodecamer. The protomer features an N-terminal β-barrel, a catalytic domain, a β-hairpin thumb, and a unique iron-finger motif. The iron-finger motif contributes to back-to-back dimerization; six dimers form the ring through β-hairpin thumb-mediated hand-in-hand contact. The structure of ADP-D-glycero-β-D-manno-heptose (ADP-D,D-heptose)-bound TibC reveals a sugar transfer mechanism and also the ligand stereoselectivity determinant. Electron-cryomicroscopy analyses uncover a TibC-TibA dodecamer/hexamer assembly with two enzyme molecules binding to one TibA substrate. The complex structure also highlights a high efficient hyperglycosylation of six autotransporter substrates simultaneously by the dodecamer enzyme complex. |
リンク | Elife / PubMed:25310236 / PubMed Central |
手法 | EM (単粒子) / X線回折 |
解像度 | 2.881 - 11.5 Å |
構造データ | EMDB-2755: EMDB-2756: EMDB-2757: EMDB-2758: PDB-4rap: PDB-4rb4: |
化合物 | ChemComp-FE: ChemComp-EDO: ChemComp-HOH: ChemComp-AQH: |
由来 |
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キーワード | TRANSFERASE (転移酵素) / GT-B fold / TibA / ADP-heptose / Heptose transfer / ADP-D-beta-D-heptose |