2h7o

</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>

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== 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<ref>PMID:16959567</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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