A structural mechanism for bacterial autotransporter glycosylation by a dodecameric heptosyltransferase family
- National Institute of Biological Sciences, China
- Institute of Biophysics, Chinese Academy of Sciences, China
- Peking University, China
- University of Natural Resources and Life Sciences, Austria
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 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 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. 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.
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© 2014, Yao et al.
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A structural mechanism for bacterial autotransporter glycosylation by a dodecameric heptosyltransferase family
eLife 3:e03714.
https://doi.org/10.7554/eLife.03714
