SopB is a Type III secreted Salmonella effector protein with phosphoinositide phosphatase activity and a GTPase binding domain that interacts with host Cdc42, an essential Rho GTPase that regulates critical events in eukaryotic cytoskeleton organization and membrane trafficking. Structural and biochemical analysis of the SopB GTPase binding domain in complex with Cdc42 shows for the first time that SopB structurally and functionally mimics a host guanine nucleotide dissociation inhibitor (GDI) by contacting key residues in the regulatory switch regions of Cdc42 and slowing Cdc42 nucleotide exchange.
Structure of Salmonella Effector Protein SopB N-terminal domain in complex with Host Rho GTPase Cdc42.,Burkinshaw B, Strynadka NC J Biol Chem. 2012 Feb 23. PMID:22362774[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
