2h7o

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Revision as of 09:28, 21 November 2007

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spinqualitylabelsall models 2h7o, resolution 2.000Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of the Rho-GTPase binding domain of YpkA

Overview

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.

About this Structure

2H7O is a Single protein structure of sequence from Yersinia pseudotuberculosis. Full crystallographic information is available from OCA.

Reference

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

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