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TitleA structural mechanism for bacterial autotransporter glycosylation by a dodecameric heptosyltransferase family.
Journal, issue, pagesElife, Vol. 3, Year 2014
Publish dateOct 13, 2014
AuthorsQing Yao / Qiuhe Lu / Xiaobo Wan / Feng Song / Yue Xu / Mo Hu / Alla Zamyatina / Xiaoyun Liu / Niu Huang / Ping Zhu / Feng Shao /
PubMed AbstractA 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.
External linksElife / PubMed:25310236 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.881 - 11.5 Å
Structure data

EMDB-2755:
Cryo-electron microscopy of TibC dodecamer
Method: EM (single particle) / Resolution: 11.5 Å

EMDB-2756:
Cryo-electron microscopy of TibC12-TibA6 octadecamer in averaged conformation
Method: EM (single particle) / Resolution: 9.7 Å

EMDB-2757:
Cryo-electron microscopy of TibC12-TibA6 octadecamer in active state
Method: EM (single particle) / Resolution: 8.2 Å

EMDB-2758:
Cryo-electron microscopy of TibC12-TibA6 octadecamer in resting state
Method: EM (single particle) / Resolution: 8.9 Å

PDB-4rap:
Crystal structure of bacterial iron-containing dodecameric glycosyltransferase TibC from enterotoxigenic E.coli H10407
Method: X-RAY DIFFRACTION / Resolution: 2.881 Å

PDB-4rb4:
Crystal structure of dodecameric iron-containing heptosyltransferase TibC in complex with ADP-D-beta-D-heptose at 3.9 angstrom resolution
Method: X-RAY DIFFRACTION / Resolution: 3.88 Å

Chemicals

ChemComp-FE:
Unknown entry

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-AQH:
[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl (2R,3R,4R,5R,6S)-6-[(1R)-1,2-dihydroxyethyl]-3,4,5-trihydroxytetrahydro-2H-pyran-2-yl dihydrogen diphosphate

Source
  • escherichia coli etec h10407 (bacteria)
  • escherichia coli dec13e (bacteria)
KeywordsTRANSFERASE / GT-B fold / TibA / ADP-heptose / Heptose transfer / ADP-D-beta-D-heptose

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