1g4u
From Proteopedia
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CRYSTAL STRUCTURE OF THE SALMONELLA TYROSINE PHOSPHATASE AND GTPASE ACTIVATING PROTEIN SPTP BOUND TO RAC1
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
1G4U is a Protein complex structure of sequences from Homo sapiens and Salmonella typhimurium with MG, GDP and AF3 as ligands. 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
Page seeded by OCA on Mon Nov 12 17:00:44 2007
Categories: Homo sapiens | Protein complex | Salmonella typhimurium | Galan, J.E. | Stebbins, C.E. | AF3 | GDP | MG | 4-helix bundle | Gap | Gtpase | Tyrosine phosphatase | Virulence factor
