4q1q: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<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>
<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='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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.11&#8491;</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>, <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'>[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>
</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>  
[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;">
== Publication Abstract from PubMed ==
Autotransporters 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<ref>PMID:25211077</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4q1q" style="background-color:#fffaf0;"></div>
== References ==
== References ==
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