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


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 ?-barrel, a catalytic domain, a ?-hairpin thumb, and a unique iron-finger motif. The iron-finger motif contributes to back-to-back dimerization; six dimers form the ring through ?-hairpin thumb-mediated hand-in-hand contact. The structure of ADP-D-glycero-?-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.

SUBMITTER: Yao Q 

PROVIDER: S-EPMC4358343 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature

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

Yao Qing Q   Lu Qiuhe Q   Wan Xiaobo X   Song Feng F   Xu Yue Y   Hu Mo M   Zamyatina Alla A   Liu Xiaoyun X   Huang Niu N   Zhu Ping P   Shao Feng F  

eLife 20141013


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-barr  ...[more]

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