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

Publication Type:

Journal Article

Authors:

Germane, Katherine L; Spiller, Benjamin W

Source:

Biochemistry, Volume 50, Issue 6, p.917-9 (2011)

Keywords:

Binding Sites, Enteropathogenic Escherichia coli, Escherichia coli Proteins, Models, Molecular, p21-Activated Kinases, Protein Conformation, Structure-Activity Relationship, Virulence Factors

Abstract:

<p>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.</p>