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Title | A structural mechanism for bacterial autotransporter glycosylation by a dodecameric heptosyltransferase family. |
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Journal, issue, pages | Elife, Vol. 3, Year 2014 |
Publish date | Oct 13, 2014 |
![]() | Qing Yao / Qiuhe Lu / Xiaobo Wan / Feng Song / Yue Xu / Mo Hu / Alla Zamyatina / Xiaoyun Liu / Niu Huang / Ping Zhu / Feng Shao / ![]() ![]() |
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. ...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. |
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Methods | EM (single particle) / X-ray diffraction |
Resolution | 2.881 - 11.5 Å |
Structure data | ![]() EMDB-2755: ![]() EMDB-2756: ![]() EMDB-2757: ![]() EMDB-2758: ![]() PDB-4rap: ![]() PDB-4rb4: |
Chemicals | ![]() ChemComp-FE: ![]() ChemComp-EDO: ![]() ChemComp-HOH: ![]() ChemComp-AQH: |
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