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Biochemistry. 2011 Feb 15;50(6):917-9. doi: 10.1021/bi1020138. Epub 2011 Jan 24.

Structural and functional studies indicate that the EPEC effector, EspG, directly binds p21-activated kinase.

Author information

1
Department of Microbiology and Immunology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232, United States.

Abstract

Bacterial pathogens secrete effectors into their hosts that subvert host defenses and redirect host processes. EspG is a type three secretion effector with a disputed function that is found in enteropathogenic Escherichia coli. Here we show that EspG is structurally similar to VirA, a Shigella virulence factor; EspG has a large, conserved pocket on its surface; EspG binds directly to the amino-terminal inhibitory domain of human p21-activated kinase (PAK); and mutations to conserved residues in the surface pocket disrupt the interaction with PAK.

PMID:
21235237
PMCID:
PMC3040069
DOI:
10.1021/bi1020138
[Indexed for MEDLINE]
Free PMC Article

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