4q1q: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q1q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q1q RCSB], [http://www.ebi.ac.uk/pdbsum/4q1q PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q1q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q1q RCSB], [http://www.ebi.ac.uk/pdbsum/4q1q PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== 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> | |||
<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: Lu, Q | [[Category: Lu, Q]] | ||
[[Category: Shao, F | [[Category: Shao, F]] | ||
[[Category: Yao, Q | [[Category: Yao, Q]] | ||
[[Category: Adhesion]] | [[Category: Adhesion]] | ||
[[Category: Beta-helix]] | [[Category: Beta-helix]] | ||
[[Category: Cell adhesion]] | [[Category: Cell adhesion]] | ||
Revision as of 12:44, 25 December 2014
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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