6gbh: Difference between revisions
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==Helicobacter pylori adhesin HopQ type II bound to the N-terminal domain of human CEACAM1== | ==Helicobacter pylori adhesin HopQ type II bound to the N-terminal domain of human CEACAM1== | ||
<StructureSection load='6gbh' size='340' side='right' caption='[[6gbh]], [[Resolution|resolution]] 2.59Å' scene=''> | <StructureSection load='6gbh' size='340' side='right'caption='[[6gbh]], [[Resolution|resolution]] 2.59Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6gbh]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6gbh]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GBH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GBH 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]] 2.59Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6gbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gbh OCA], [https://pdbe.org/6gbh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gbh RCSB], [https://www.ebi.ac.uk/pdbsum/6gbh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6gbh ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/CEAM1_HUMAN CEAM1_HUMAN] | |||
<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: Helicobacter pylori]] | [[Category: Helicobacter pylori]] | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Gerhard M]] | |||
[[Category: Kruse T]] | |||
[[Category: Moonens K]] | |||
[[Category: Remaut H]] | |||
Latest revision as of 15:40, 6 November 2024
Helicobacter pylori adhesin HopQ type II bound to the N-terminal domain of human CEACAM1Helicobacter pylori adhesin HopQ type II bound to the N-terminal domain of human CEACAM1
Structural highlights
FunctionPublication Abstract from PubMedThe human gastric pathogen Helicobacter pylori is a major causative agent of gastritis, peptic ulcer disease, and gastric cancer. As part of its adhesive lifestyle, the bacterium targets members of the carcinoembryonic antigen-related cell adhesion molecule (CEACAM) family by the conserved outer membrane adhesin HopQ. The HopQ-CEACAM1 interaction is associated with inflammatory responses and enables the intracellular delivery and phosphorylation of the CagA oncoprotein via a yet unknown mechanism. Here, we generated crystal structures of HopQ isotypes I and II bound to the N-terminal domain of human CEACAM1 (C1ND) and elucidated the structural basis of H. pylori specificity toward human CEACAM receptors. Both HopQ alleles target the beta-strands G, F, and C of C1ND, which form the trans dimerization interface in homo- and heterophilic CEACAM interactions. Using SAXS, we show that the HopQ ectodomain is sufficient to induce C1ND monomerization and thus providing H. pylori a route to influence CEACAM-mediated cell adherence and signaling events. Helicobacter pylori adhesin HopQ disrupts trans dimerization in human CEACAMs.,Moonens K, Hamway Y, Neddermann M, Reschke M, Tegtmeyer N, Kruse T, Kammerer R, Mejias-Luque R, Singer BB, Backert S, Gerhard M, Remaut H EMBO J. 2018 Jun 1. pii: embj.201798665. doi: 10.15252/embj.201798665. PMID:29858229[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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