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J Biol Chem. 2012 Apr 13;287(16):13348-55. doi: 10.1074/jbc.M111.331330. Epub 2012 Feb 23.

Structure of Salmonella effector protein SopB N-terminal domain in complex with host Rho GTPase Cdc42.

Author information

1
Department of Biochemistry and Molecular Biology and Center for Blood Research, University of British Columbia, Vancouver, British Columbia V6T 1Z3, Canada.

Abstract

SopB is a type III secreted Salmonella effector protein with phosphoinositide phosphatase activity and a distinct GTPase binding domain. The latter 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.

PMID:
22362774
PMCID:
PMC3339929
DOI:
10.1074/jbc.M111.331330
[Indexed for MEDLINE]
Free PMC Article
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