A structural mechanism for bacterial autotransporter glycosylation by a   dodecameric heptosyltransferase family

doi:10.7554/eLife.03714

CORC > 北京大学 > 化学与分子工程学院

	A structural mechanism for bacterial autotransporter glycosylation by a dodecameric heptosyltransferase family
	Yao, Qing ; Lu, Qiuhe ; Wan, Xiaobo ; Song, Feng ; Xu, Yue ; Hu, Mo ; Zamyatina, Alla ; Liu, Xiaoyun ; Huang, Niu ; Zhu, Ping ; Shao, Feng
刊名	elife
	2014
关键词	ENTEROTOXIGENIC ESCHERICHIA-COLI PARTICLE ELECTRON CRYOMICROSCOPY MOLECULAR-DYNAMICS SIMULATIONS EM STRUCTURE DETERMINATION PROTEIN GLYCOSYLATION SIDE-CHAIN CLOSTRIDIUM-PASTEURIANUM DIFFUSE ADHERENCE GLYCOSYLTRANSFERASES ADHESIN
DOI	10.7554/eLife.03714
英文摘要	A large group of bacterial virulence autotransporters including AIDA-I from diffusely adhering E. coli (DAEC) and TibA from enterotoxigenic E. coli (ETEC) require hyper-glycosylation 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). Crystal structure of TibC reveals a characteristic ring-shape dodecamer. The protomer features an N-terminal beta-barrel, a catalytic domain, a beta-hairpin thumb and a unique iron-finger motif The iron-finger motif contributes to back-to-back dimerization; six dimers form the ring through beta-hairpin thumb-mediated hand-in-hand contact. Structure of ADP-D, D-heptose-bound TibC reveals a sugar transfer mechanism and also the ligand stereoselectivity determinant. Cryo-EM 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.; Biology; SCI(E); PubMed; 0; ARTICLE; shaofeng@nibs.ac.cn; 3
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/342081]
专题	化学与分子工程学院
推荐引用方式 GB/T 7714	Yao, Qing,Lu, Qiuhe,Wan, Xiaobo,et al. A structural mechanism for bacterial autotransporter glycosylation by a dodecameric heptosyltransferase family[J]. elife,2014.
APA	Yao, Qing.,Lu, Qiuhe.,Wan, Xiaobo.,Song, Feng.,Xu, Yue.,...&Shao, Feng.(2014).A structural mechanism for bacterial autotransporter glycosylation by a dodecameric heptosyltransferase family.elife.
MLA	Yao, Qing,et al."A structural mechanism for bacterial autotransporter glycosylation by a dodecameric heptosyltransferase family".elife (2014).