4rap: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4rap]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_ETEC_H10407 Escherichia coli ETEC H10407]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RAP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RAP FirstGlance]. <br> | <table><tr><td colspan='2'>[[4rap]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_ETEC_H10407 Escherichia coli ETEC H10407]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RAP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RAP FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.881Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4rap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rap OCA], [https://pdbe.org/4rap PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rap RCSB], [https://www.ebi.ac.uk/pdbsum/4rap PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rap ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4rap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rap OCA], [https://pdbe.org/4rap PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rap RCSB], [https://www.ebi.ac.uk/pdbsum/4rap PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rap ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 11:30, 9 October 2024
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
FunctionTIBC_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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