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| ==Helicobacter pylori adhesin HopQ type I bound to the N-terminal domain of human CEACAM1== | | ==Helicobacter pylori adhesin HopQ type I bound to the N-terminal domain of human CEACAM1== |
- | <StructureSection load='6gbg' size='340' side='right' caption='[[6gbg]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='6gbg' size='340' side='right'caption='[[6gbg]], [[Resolution|resolution]] 2.80Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[6gbg]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Helpg Helpg] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GBG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GBG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6gbg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_G27 Helicobacter pylori G27] 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=6GBG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GBG FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</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]] 2.8Å</td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CEACAM1, BGP, BGP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), hopQ, HPG27_1120 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=563041 HELPG])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></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=6gbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gbg OCA], [http://pdbe.org/6gbg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gbg RCSB], [http://www.ebi.ac.uk/pdbsum/6gbg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gbg 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=6gbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gbg OCA], [https://pdbe.org/6gbg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gbg RCSB], [https://www.ebi.ac.uk/pdbsum/6gbg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6gbg 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: Helpg]] | + | [[Category: Helicobacter pylori G27]] |
- | [[Category: Human]] | + | [[Category: Homo sapiens]] |
- | [[Category: Gerhard, M]] | + | [[Category: Large Structures]] |
- | [[Category: Kruse, T]] | + | [[Category: Gerhard M]] |
- | [[Category: Moonens, K]] | + | [[Category: Kruse T]] |
- | [[Category: Remaut, H]] | + | [[Category: Moonens K]] |
- | [[Category: Adhesin]]
| + | [[Category: Remaut H]] |
- | [[Category: Cell adhesion]]
| + | |
- | [[Category: Helicobacter outer membrane protein]]
| + | |
- | [[Category: Helicobacter pylori]]
| + | |
| Structural highlights
Function
CEAM1_HUMAN
Publication Abstract from PubMed
The 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
- ↑ 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. Helicobacter pylori adhesin HopQ disrupts trans dimerization in human CEACAMs. EMBO J. 2018 Jun 1. pii: embj.201798665. doi: 10.15252/embj.201798665. PMID:29858229 doi:http://dx.doi.org/10.15252/embj.201798665
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