Structural and Functional Studies Indicate That the EPEC Effector, EspG, Directly Binds p21-Activated Kinase
Year: 2011
Type: article
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.
Source: Biochemistry
DOI: 10.1021/bi1020138
Authors: Katherine L. Germane, Benjamin W. Spiller
Institution: Vanderbilt University
Language: English
Subfield: Endocrinology
Domain: Life Sciences
Open Access status: green
Awards: G1764958080, Molecular Biophysics Training Grant at Vanderbilt, G2861424750, G3834503677, G5058979636, The Vanderbilt Institute for Clinical and Translational Research (VICTR) KL2, An Undulator Resource for Structural Biology, The Vanderbilt Institute for Clinical and Translational Research (VICTR) TL1, The Vanderbilt Institute for Clinical and Translational Research (VICTR) UL1, Molecular and Cellular Basis for Digestive Diseases
OpenAlex ID: W2090970490