4q1q: Difference between revisions
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<StructureSection load='4q1q' size='340' side='right'caption='[[4q1q]], [[Resolution|resolution]] 2.11Å' scene=''> | <StructureSection load='4q1q' size='340' side='right'caption='[[4q1q]], [[Resolution|resolution]] 2.11Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4q1q]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4q1q]] is a 2 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=4Q1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q1Q FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.11Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=289:D-GLYCERO-ALPHA-D-MANNO-HEPTOPYRANOSE'>289</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=4q1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q1q OCA], [https://pdbe.org/4q1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q1q RCSB], [https://www.ebi.ac.uk/pdbsum/4q1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q1q ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/TIBA_ECOH1 TIBA_ECOH1] Mediates both adhesion to and invasion of human intestine epithelial cells. Also mediates bacterial cell aggregation via intercellular TibA-TibA interaction. Enhances biofilm formation.<ref>PMID:11119488</ref> <ref>PMID:8039917</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli ETEC H10407]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Lu | [[Category: Lu Q]] | ||
[[Category: Shao | [[Category: Shao F]] | ||
[[Category: Yao | [[Category: Yao Q]] | ||
Latest revision as of 14:18, 6 November 2024
Crystal structure of TibC-catalyzed hyper-glycosylated TibA55-350 fragmentCrystal structure of TibC-catalyzed hyper-glycosylated TibA55-350 fragment
Structural highlights
FunctionTIBA_ECOH1 Mediates both adhesion to and invasion of human intestine epithelial cells. Also mediates bacterial cell aggregation via intercellular TibA-TibA interaction. Enhances biofilm formation.[1] [2] Publication Abstract from PubMedAutotransporters deliver virulence factors to the bacterial surface by translocating an effector passenger domain through a membrane-anchored barrel structure. Although passenger domains are diverse, those found in enteric bacteria autotransporters, including AIDA-I in diffusely adhering Escherichia coli (DAEC) and TibA in enterotoxigenic E. coli, are commonly glycosylated. We show that AIDA-I is heptosylated within the bacterial cytoplasm by autotransporter adhesin heptosyltransferase (AAH) and its paralogue AAH2. AIDA-I heptosylation determines DAEC adhesion to host cells. AAH/AAH2 define a bacterial autotransporter heptosyltransferase (BAHT) family that contains ferric ion and adopts a dodecamer assembly. Structural analyses of the heptosylated TibA passenger domain reveal 35 heptose conjugates forming patterned and solenoid-like arrays on the surface of a beta helix. Additionally, CARC, the AIDA-like autotransporter from Citrobacter rodentium, is essential for colonization in mice and requires heptosylation by its cognate BAHT. Our study establishes a bacterial glycosylation system that regulates virulence and is essential for pathogenesis. An iron-containing dodecameric heptosyltransferase family modifies bacterial autotransporters in pathogenesis.,Lu Q, Yao Q, Xu Y, Li L, Li S, Liu Y, Gao W, Niu M, Sharon M, Ben-Nissan G, Zamyatina A, Liu X, Chen S, Shao F Cell Host Microbe. 2014 Sep 10;16(3):351-63. doi: 10.1016/j.chom.2014.08.008. PMID:25211077[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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