1g4u
From Proteopedia
|
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 , and 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 Thu Feb 21 12:46:06 2008
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
