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==Crystal structure of bacterial iron-containing dodecameric glycosyltransferase TibC from enterotoxigenic E.coli H10407== | ==Crystal structure of bacterial iron-containing dodecameric glycosyltransferase TibC from enterotoxigenic E.coli H10407== | ||
<StructureSection load='4rap' size='340' side='right' caption='[[4rap]], [[Resolution|resolution]] 2.88Å' scene=''> | <StructureSection load='4rap' size='340' side='right' caption='[[4rap]], [[Resolution|resolution]] 2.88Å' scene=''> | ||
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4q1q|4q1q]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4q1q|4q1q]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4rap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rap OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rap RCSB], [http://www.ebi.ac.uk/pdbsum/4rap PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4rap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rap OCA], [http://pdbe.org/4rap PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rap RCSB], [http://www.ebi.ac.uk/pdbsum/4rap PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rap ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4rap" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Glycosyltransferase|Glycosyltransferase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 01:25, 5 August 2016
Crystal structure of bacterial iron-containing dodecameric glycosyltransferase TibC from enterotoxigenic E.coli H10407Crystal structure of bacterial iron-containing dodecameric glycosyltransferase TibC from enterotoxigenic E.coli H10407
Structural highlights
Function[TIBC_ECOH1] Glycosylates the TibA adhesin. Publication Abstract from PubMedA 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. A structural mechanism for bacterial autotransporter glycosylation by a dodecameric heptosyltransferase family.,Yao Q, Lu Q, Wan X, Song F, Xu Y, Hu M, Zamyatina A, Liu X, Huang N, Zhu P, Shao F Elife. 2014 Oct 13;3. doi: 10.7554/eLife.03714. PMID:25310236[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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