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| | ==Crystal structure of the N-terminal domain of Helicobacter pylori CagA protein== | | ==Crystal structure of the N-terminal domain of Helicobacter pylori CagA protein== |
| - | <StructureSection load='4g0h' size='340' side='right' caption='[[4g0h]], [[Resolution|resolution]] 3.60Å' scene=''> | + | <StructureSection load='4g0h' size='340' side='right'caption='[[4g0h]], [[Resolution|resolution]] 3.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4g0h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Campylobacter_pylori Campylobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G0H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4G0H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4g0h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori_26695 Helicobacter pylori 26695]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4G0H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4G0H FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">cag26, cagA, cai, HP0547, HP_0547 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=85962 Campylobacter pylori])</td></tr> | + | </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=4g0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g0h OCA], [https://pdbe.org/4g0h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4g0h RCSB], [https://www.ebi.ac.uk/pdbsum/4g0h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4g0h ProSAT]</span></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=4g0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g0h OCA], [http://pdbe.org/4g0h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4g0h RCSB], [http://www.ebi.ac.uk/pdbsum/4g0h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4g0h ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CAGA_HELPY CAGA_HELPY]] May be necessary for the transcription, folding, export, or function of the cytotoxin. | + | [https://www.uniprot.org/uniprot/CAGA_HELPY CAGA_HELPY] May be necessary for the transcription, folding, export, or function of the cytotoxin. |
| | <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: Campylobacter pylori]] | + | [[Category: Helicobacter pylori 26695]] |
| - | [[Category: Dian, C]] | + | [[Category: Large Structures]] |
| - | [[Category: Kaplan-Turkoz, B]] | + | [[Category: Dian C]] |
| - | [[Category: Louche, A]] | + | [[Category: Kaplan-Turkoz B]] |
| - | [[Category: Remaut, H]] | + | [[Category: Louche A]] |
| - | [[Category: Terradot, L]] | + | [[Category: Remaut H]] |
| - | [[Category: Cytotoxin]]
| + | [[Category: Terradot L]] |
| - | [[Category: Integrin beta 1]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Toxin]]
| + | |
| Structural highlights
Function
CAGA_HELPY May be necessary for the transcription, folding, export, or function of the cytotoxin.
Publication Abstract from PubMed
Infection with the gastric pathogen Helicobacter pylori is a risk factor for the development of gastric cancer. Pathogenic strains of H. pylori carry a type IV secretion system (T4SS) responsible for the injection of the oncoprotein CagA into host cells. H. pylori and its cag-T4SS exploit alpha5beta1 integrin as a receptor for CagA translocation. Injected CagA localizes to the inner leaflet of the host cell membrane, where it hijacks host cell signaling and induces cytoskeleton reorganization. Here we describe the crystal structure of the N-terminal ~100-kDa subdomain of CagA at 3.6 A that unveils a unique combination of folds. The core domain of the protein consists of an extended single-layer beta-sheet stabilized by two independent helical subdomains. The core is followed by a long helix that forms a four-helix helical bundle with the C-terminal domain. Mapping of conserved regions in a set of CagA sequences identified four conserved surface-exposed patches (CSP1-4), which represent putative hot-spots for protein-protein interactions. The proximal part of the single-layer beta-sheet, covering CSP4, is involved in specific binding of CagA to the beta1 integrin, as determined by yeast two-hybrid and in vivo competition assays in H. pylori cell-culture infection studies. These data provide a structural basis for the first step of CagA internalization into host cells and suggest that CagA uses a previously undescribed mechanism to bind beta1 integrin to mediate its own translocation.
Structural insights into Helicobacter pylori oncoprotein CagA interaction with beta1 integrin.,Kaplan-Turkoz B, Jimenez-Soto LF, Dian C, Ertl C, Remaut H, Louche A, Tosi T, Haas R, Terradot L Proc Natl Acad Sci U S A. 2012 Sep 4;109(36):14640-5. doi:, 10.1073/pnas.1206098109. Epub 2012 Aug 20. PMID:22908298[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kaplan-Turkoz B, Jimenez-Soto LF, Dian C, Ertl C, Remaut H, Louche A, Tosi T, Haas R, Terradot L. Structural insights into Helicobacter pylori oncoprotein CagA interaction with beta1 integrin. Proc Natl Acad Sci U S A. 2012 Sep 4;109(36):14640-5. doi:, 10.1073/pnas.1206098109. Epub 2012 Aug 20. PMID:22908298 doi:10.1073/pnas.1206098109
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