1g4w
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(New page: 200px<br /><applet load="1g4w" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g4w, resolution 2.2Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 13:35, 20 November 2007
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CRYSTAL STRUCTURE OF THE SALMONELLA TYROSINE PHOSPHATASE AND GTPASE ACTIVATING PROTEIN SPTP
Overview
Salmonella spp. utilize a specialized protein secretion system to deliver, a battery of effector proteins into host cells. Several of these effectors, stimulate Cdc42- and Rac1-dependent cytoskeletal changes that promote, bacterial internalization. These potentially cytotoxic alterations are, rapidly reversed by the effector SptP, a tyrosine phosphatase and GTPase, activating protein (GAP) that targets Cdc42 and Rac1. The 2.3 A resolution, crystal structure of an SptP-Rac1 transition state complex reveals an, unusual GAP architecture that mimics host functional homologs. The, phosphatase domain possesses a conserved active site but distinct surface, properties. Binding to Rac1 induces a dramatic stabilization in SptP of a, four-helix bundle that makes extensive contacts with the Switch I and, Switch II regions of the GTPase.
About this Structure
1G4W is a Single protein structure of sequence from Salmonella typhimurium. Full crystallographic information is available from OCA.
Reference
Modulation of host signaling by a bacterial mimic: structure of the Salmonella effector SptP bound to Rac1., Stebbins CE, Galan JE, Mol Cell. 2000 Dec;6(6):1449-60. PMID:11163217
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