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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://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></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>, <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='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='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://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 == |
| - | [[http://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoh1]] | + | [[Category: Escherichia coli ETEC H10407]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lu, Q]] | + | [[Category: Lu Q]] |
| - | [[Category: Shao, F]] | + | [[Category: Shao F]] |
| - | [[Category: Yao, Q]] | + | [[Category: Yao Q]] |
| - | [[Category: Adhesion]]
| + | |
| - | [[Category: Beta-helix]]
| + | |
| - | [[Category: Cell adhesion]]
| + | |
| 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 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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lindenthal C, Elsinghorst EA. Enterotoxigenic Escherichia coli TibA glycoprotein adheres to human intestine epithelial cells. Infect Immun. 2001 Jan;69(1):52-7. PMID:11119488 doi:http://dx.doi.org/10.1128/IAI.69.1.52-57.2001
- ↑ Elsinghorst EA, Weitz JA. Epithelial cell invasion and adherence directed by the enterotoxigenic Escherichia coli tib locus is associated with a 104-kilodalton outer membrane protein. Infect Immun. 1994 Aug;62(8):3463-71. PMID:8039917
- ↑ 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. An iron-containing dodecameric heptosyltransferase family modifies bacterial autotransporters in pathogenesis. Cell Host Microbe. 2014 Sep 10;16(3):351-63. doi: 10.1016/j.chom.2014.08.008. PMID:25211077 doi:http://dx.doi.org/10.1016/j.chom.2014.08.008
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