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| | ==Structure of a SycH-YopH Chaperone-Effector Complex== | | ==Structure of a SycH-YopH Chaperone-Effector Complex== |
| - | <StructureSection load='4gf3' size='340' side='right' caption='[[4gf3]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='4gf3' size='340' side='right'caption='[[4gf3]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4gf3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pestis"_(lehmann_and_neumann_1896)_migula_1900 "bacillus pestis" (lehmann and neumann 1896) migula 1900] and [http://en.wikipedia.org/wiki/"bacterium_enterocoliticum"_schleifstein_and_coleman_1939 "bacterium enterocoliticum" schleifstein and coleman 1939]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GF3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GF3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4gf3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica] and [https://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GF3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GF3 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sycH, YP_pCD87, YPCD1.95c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=632 "Bacillus pestis" (Lehmann and Neumann 1896) Migula 1900]), yopH, yop51 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=630 "Bacterium enterocoliticum" Schleifstein and Coleman 1939])</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]] 1.9Å</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=4gf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gf3 OCA], [http://pdbe.org/4gf3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gf3 RCSB], [http://www.ebi.ac.uk/pdbsum/4gf3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gf3 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=4gf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gf3 OCA], [https://pdbe.org/4gf3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gf3 RCSB], [https://www.ebi.ac.uk/pdbsum/4gf3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gf3 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/YOPH_YEREN YOPH_YEREN]] Essential virulence determinant. This protein is a protein tyrosine phosphatase. The essential function of YopH in Yersinia pathogenesis is host-protein dephosphorylation. It contributes to the ability of the bacteria to resist phagocytosis by peritoneal macrophages. | + | [https://www.uniprot.org/uniprot/Q7BTX0_YERPE Q7BTX0_YERPE] |
| - | <div style="background-color:#fffaf0;">
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| - | == Publication Abstract from PubMed ==
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| - | Yersinia pestis injects numerous bacterial proteins into host cells through an organic nanomachine called the type 3 secretion system. One such substrate is the tyrosine phosphatase YopH, which requires an interaction with a cognate chaperone in order to be effectively injected. Here, the first crystal structure of a SycH-YopH complex is reported, determined to 1.9 A resolution. The structure reveals the presence of (i) a nonglobular polypeptide in YopH, (ii) a so-called beta-motif in YopH and (iii) a conserved hydrophobic patch in SycH that recognizes the beta-motif. Biochemical studies establish that the beta-motif is critical to the stability of this complex. Finally, since previous work has shown that the N-terminal portion of YopH adopts a globular fold that is functional in the host cell, aspects of how this polypeptide adopts radically different folds in the host and in the bacterial environments are analysed.
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| - | Context-dependent protein folding of a virulence peptide in the bacterial and host environments: structure of an SycH-YopH chaperone-effector complex.,Vujanac M, Stebbins CE Acta Crystallogr D Biol Crystallogr. 2013 Apr;69(Pt 4):546-54. doi:, 10.1107/S0907444912051086. Epub 2013 Mar 9. PMID:23519663<ref>PMID:23519663</ref>
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
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| - | <div class="pdbe-citations 4gf3" style="background-color:#fffaf0;"></div>
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| | ==See Also== | | ==See Also== |
| - | *[[Tyrosine phosphatase|Tyrosine phosphatase]] | + | *[[Tyrosine phosphatase 3D structures|Tyrosine phosphatase 3D structures]] |
| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacterium enterocoliticum schleifstein and coleman 1939]] | + | [[Category: Large Structures]] |
| - | [[Category: Stebbins, C E]] | + | [[Category: Yersinia enterocolitica]] |
| - | [[Category: Vujanac, M]] | + | [[Category: Yersinia pestis]] |
| - | [[Category: Chaperone-chaperone effector complex]] | + | [[Category: Stebbins CE]] |
| - | [[Category: T3ss chaperone]] | + | [[Category: Vujanac M]] |
