1G4W

CRYSTAL STRUCTURE OF THE SALMONELLA TYROSINE PHOSPHATASE AND GTPASE ACTIVATING PROTEIN SPTP

Summary for 1G4W

• Entry DOI: 10.2210/pdb1g4w/pdb
• Related: 1G4U
• Descriptor: PROTEIN TYROSINE PHOSPHATASE SPTP (2 entities in total)
• Functional Keywords: virulence factor, tyrosine phosphatase, gtpase activating protein, 4-helix bundle, disorder, signaling protein
• Biological source: Salmonella typhimurium
• Cellular location: Secreted : P74873
• Total number of polymer chains: 1
• Total formula weight: 42127.80

Authors

Stebbins, C.E.,Galan, J.E. (deposition date: 2000-10-28, release date: 2001-01-24, Last modification date: 2024-02-07)

Primary citation

Stebbins, C.E.,Galan, J.E.
Modulation of host signaling by a bacterial mimic: structure of the Salmonella effector SptP bound to Rac1.
Mol.Cell, 6:1449-1460, 2000

PubMed Abstract: 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.

PubMed: 11163217
DOI: 10.1016/S1097-2765(00)00141-6

Experimental method

X-RAY DIFFRACTION (2.2 Å)