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6gbh

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'''Unreleased structure'''
 
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The entry 6gbh is ON HOLD until Paper Publication
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==Helicobacter pylori adhesin HopQ type II bound to the N-terminal domain of human CEACAM1==
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<StructureSection load='6gbh' size='340' side='right' caption='[[6gbh]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6gbh]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504] and [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GBH FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<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 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 ATCC 43504])</td></tr>
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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=6gbh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gbh OCA], [http://pdbe.org/6gbh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gbh RCSB], [http://www.ebi.ac.uk/pdbsum/6gbh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gbh ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Moonens, K., Kruse, T., Gerhard, M., Remaut, H.
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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<ref>PMID:29858229</ref>
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Description: Helicobacter pylori adhesin HopQ type II bound to the N-terminal domain of human CEACAM1
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Remaut, H]]
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<div class="pdbe-citations 6gbh" style="background-color:#fffaf0;"></div>
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[[Category: Moonens, K]]
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== References ==
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[[Category: Kruse, T]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Atcc 43504]]
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[[Category: Human]]
[[Category: Gerhard, M]]
[[Category: Gerhard, M]]
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[[Category: Kruse, T]]
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[[Category: Moonens, K]]
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[[Category: Remaut, H]]
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[[Category: Adhesin]]
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[[Category: Cell adhesion]]
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[[Category: Helicobacter outer membrane protein]]
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[[Category: Helicobacter pylori]]

Current revision

Helicobacter pylori adhesin HopQ type II bound to the N-terminal domain of human CEACAM1

6gbh, resolution 2.59Å

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