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| | ==Crystal structure of the Rho-GTPase binding domain of YpkA== | | ==Crystal structure of the Rho-GTPase binding domain of YpkA== |
| - | <StructureSection load='2h7o' size='340' side='right' caption='[[2h7o]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='2h7o' size='340' side='right'caption='[[2h7o]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2h7o]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_pseudotuberkulosis"_(sic)_pfeiffer_1889 "bacillus pseudotuberkulosis" (sic) pfeiffer 1889]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H7O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2H7O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2h7o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_pseudotuberkulosis"_(sic)_pfeiffer_1889 "bacillus pseudotuberkulosis" (sic) pfeiffer 1889]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H7O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H7O FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ypkA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=633 "Bacillus pseudotuberkulosis" (sic) Pfeiffer 1889])</td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ypkA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=633 "Bacillus pseudotuberkulosis" (sic) Pfeiffer 1889])</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=2h7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h7o OCA], [http://pdbe.org/2h7o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2h7o RCSB], [http://www.ebi.ac.uk/pdbsum/2h7o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2h7o 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=2h7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h7o OCA], [https://pdbe.org/2h7o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h7o RCSB], [https://www.ebi.ac.uk/pdbsum/2h7o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h7o ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/YPKA_YERPS YPKA_YERPS]] Acts as a virulence determinant.<ref>PMID:10920208</ref> <ref>PMID:17531806</ref> | + | [[https://www.uniprot.org/uniprot/YPKA_YERPS YPKA_YERPS]] Acts as a virulence determinant.<ref>PMID:10920208</ref> <ref>PMID:17531806</ref> |
| | <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: Large Structures]] |
| | [[Category: Bliska, J B]] | | [[Category: Bliska, J B]] |
| | [[Category: Ivanov, M]] | | [[Category: Ivanov, M]] |
| Structural highlights
Function
[YPKA_YERPS] Acts as a virulence determinant.[1] [2]
Publication Abstract from PubMed
Yersinia spp. cause gastroenteritis and the plague, representing historically devastating pathogens that are currently an important biodefense and antibiotic resistance concern. A critical virulence determinant is the Yersinia protein kinase A, or YpkA, a multidomain protein that disrupts the eukaryotic actin cytoskeleton. Here we solve the crystal structure of a YpkA-Rac1 complex and find that YpkA possesses a Rac1 binding domain that mimics host guanidine nucleotide dissociation inhibitors (GDIs) of the Rho GTPases. YpkA inhibits nucleotide exchange in Rac1 and RhoA, and mutations that disrupt the YpkA-GTPase interface abolish this activity in vitro and impair in vivo YpkA-induced cytoskeletal disruption. In cell culture experiments, the kinase and the GDI domains of YpkA act synergistically to promote cytoskeletal disruption, and a Y. pseudotuberculosis mutant lacking YpkA GDI activity shows attenuated virulence in a mouse infection assay. We conclude that virulence in Yersinia depends strongly upon mimicry of host GDI proteins by YpkA.
Yersinia virulence depends on mimicry of host Rho-family nucleotide dissociation inhibitors.,Prehna G, Ivanov MI, Bliska JB, Stebbins CE Cell. 2006 Sep 8;126(5):869-80. PMID:16959567[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Juris SJ, Rudolph AE, Huddler D, Orth K, Dixon JE. A distinctive role for the Yersinia protein kinase: actin binding, kinase activation, and cytoskeleton disruption. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9431-6. PMID:10920208 doi:http://dx.doi.org/10.1073/pnas.170281997
- ↑ Navarro L, Koller A, Nordfelth R, Wolf-Watz H, Taylor S, Dixon JE. Identification of a molecular target for the Yersinia protein kinase A. Mol Cell. 2007 May 25;26(4):465-77. PMID:17531806 doi:http://dx.doi.org/S1097-2765(07)00285-7
- ↑ Prehna G, Ivanov MI, Bliska JB, Stebbins CE. Yersinia virulence depends on mimicry of host Rho-family nucleotide dissociation inhibitors. Cell. 2006 Sep 8;126(5):869-80. PMID:16959567 doi:10.1016/j.cell.2006.06.056
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