6aw2
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 6aw2 is ON HOLD until Paper Publication Authors: Bonsor, D.A., Sundberg, E.J. Description: Crystal structure of the HopQ-CEACAM1 complex [[Category...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the HopQ-CEACAM1 complex== | |
| + | <StructureSection load='6aw2' size='340' side='right'caption='[[6aw2]], [[Resolution|resolution]] 2.68Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6aw2]] is a 2 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=6AW2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AW2 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.68Å</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=6aw2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aw2 OCA], [https://pdbe.org/6aw2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6aw2 RCSB], [https://www.ebi.ac.uk/pdbsum/6aw2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6aw2 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CEAM1_HUMAN CEAM1_HUMAN] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Helicobacter pylori infects half of the world's population, and strains that encode the cag type IV secretion system for injection of the oncoprotein CagA into host gastric epithelial cells are associated with elevated levels of cancer. CagA translocation into host cells is dependent on interactions between the H. pylori adhesin protein HopQ and human CEACAMs. Here, we present high-resolution structures of several HopQ-CEACAM complexes and CEACAMs in their monomeric and dimeric forms establishing that HopQ uses a coupled folding and binding mechanism to engage the canonical CEACAM dimerization interface for CEACAM recognition. By combining mutagenesis with biophysical and functional analyses, we show that the modes of CEACAM recognition by HopQ and CEACAMs themselves are starkly different. Our data describe precise molecular mechanisms by which microbes exploit host CEACAMs for infection and enable future development of novel oncoprotein translocation inhibitors and H. pylori-specific antimicrobial agents. | ||
| - | + | The Helicobacter pylori adhesin protein HopQ exploits the dimer interface of human CEACAMs to facilitate translocation of the oncoprotein CagA.,Bonsor DA, Zhao Q, Schmidinger B, Weiss E, Wang J, Deredge D, Beadenkopf R, Dow B, Fischer W, Beckett D, Wintrode PL, Haas R, Sundberg EJ EMBO J. 2018 May 3. pii: embj.201798664. doi: 10.15252/embj.201798664. PMID:29724755<ref>PMID:29724755</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Bonsor | + | <div class="pdbe-citations 6aw2" style="background-color:#fffaf0;"></div> |
| - | [[Category: Sundberg | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Helicobacter pylori]] | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bonsor DA]] | ||
| + | [[Category: Sundberg EJ]] | ||
Current revision
Crystal structure of the HopQ-CEACAM1 complex
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