6aw3: Difference between revisions

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==Crystal structure of the HopQ-CEACAM3 L44Q complex==
==Crystal structure of the HopQ-CEACAM3 L44Q complex==
<StructureSection load='6aw3' size='340' side='right' caption='[[6aw3]], [[Resolution|resolution]] 2.66&Aring;' scene=''>
<StructureSection load='6aw3' size='340' side='right'caption='[[6aw3]], [[Resolution|resolution]] 2.66&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6aw3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AW3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AW3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[6aw3]] 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=6AW3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AW3 FirstGlance]. <br>
</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=6aw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aw3 OCA], [http://pdbe.org/6aw3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6aw3 RCSB], [http://www.ebi.ac.uk/pdbsum/6aw3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6aw3 ProSAT]</span></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]] 2.66&#8491;</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=6aw3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aw3 OCA], [https://pdbe.org/6aw3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6aw3 RCSB], [https://www.ebi.ac.uk/pdbsum/6aw3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6aw3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CEAM3_HUMAN CEAM3_HUMAN]] Major granulocyte receptor mediating recognition and efficient opsonin-independent phagocytosis of CEACAM-binding microorganisms, including Neissiria, Moxarella and Haemophilus species, thus playing an important role in the clearance of pathogens by the innate immune system. Responsible for RAC1 stimulation in the course of pathogen phagocytosis.<ref>PMID:12864848</ref> <ref>PMID:14707113</ref> 
[https://www.uniprot.org/uniprot/H6A3H4_HELPX H6A3H4_HELPX]  
<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: Bonsor, D A]]
[[Category: Helicobacter pylori]]
[[Category: Sundberg, E J]]
[[Category: Homo sapiens]]
[[Category: Cell adhesion]]
[[Category: Large Structures]]
[[Category: Bonsor DA]]
[[Category: Sundberg EJ]]

Latest revision as of 15:26, 6 November 2024

Crystal structure of the HopQ-CEACAM3 L44Q complexCrystal structure of the HopQ-CEACAM3 L44Q complex

Structural highlights

6aw3 is a 2 chain structure with sequence from Helicobacter pylori and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.66Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

H6A3H4_HELPX

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. 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. The Helicobacter pylori adhesin protein HopQ exploits the dimer interface of human CEACAMs to facilitate translocation of the oncoprotein CagA. EMBO J. 2018 May 3. pii: embj.201798664. doi: 10.15252/embj.201798664. PMID:29724755 doi:http://dx.doi.org/10.15252/embj.201798664

6aw3, resolution 2.66Å

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