4RAP

Crystal structure of bacterial iron-containing dodecameric glycosyltransferase TibC from enterotoxigenic E.coli H10407

4RAP の概要

• エントリーDOI: 10.2210/pdb4rap/pdb
• 関連するPDBエントリー: 4Q1Q
• 分子名称: Glycosyltransferase TibC, FE (III) ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: gt-b fold, transferase, tiba, adp-heptose
• 由来する生物種: Escherichia coli ETEC H10407
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 555042.46

構造登録者

Yao, Q.,Lu, Q.,Xu, Y.,Shao, F. (登録日: 2014-09-10, 公開日: 2014-10-29, 最終更新日: 2024-10-09)

主引用文献

Yao, Q.,Lu, Q.,Wan, X.,Song, F.,Xu, Y.,Hu, M.,Zamyatina, A.,Liu, X.,Huang, N.,Zhu, P.,Shao, F.
A structural mechanism for bacterial autotransporter glycosylation by a dodecameric heptosyltransferase family.
Elife, 3:-, 2014

PubMed Abstract: 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.

PubMed: 25310236
DOI: 10.7554/eLife.03714

実験手法

X-RAY DIFFRACTION (2.881 Å)