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 [http://en.wikipedia.org/wiki/Ecoh1 Ecoh1]. 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 [http:// | <table><tr><td colspan='2'>[[4q1q]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoh1 Ecoh1]. 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 [http://proteopedia.org/fgij/fg.htm?mol=4Q1Q FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=289:D-GLYCERO-ALPHA-D-MANNO-HEPTOPYRANOSE'>289</scene></td></tr> | </td></tr><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></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='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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tibA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=316401 ECOH1])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tibA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=316401 ECOH1])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=4q1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q1q OCA], [http://pdbe.org/4q1q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4q1q RCSB], [http://www.ebi.ac.uk/pdbsum/4q1q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4q1q ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
Revision as of 09:44, 25 June 2020
Crystal structure of TibC-catalyzed hyper-glycosylated TibA55-350 fragmentCrystal structure of TibC-catalyzed hyper-glycosylated TibA55-350 fragment
Structural highlights
Function[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.[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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