title: Structural and functional studies indicate that the EPEC effector, EspG, directly binds p21-activated kinase.
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.
authors.affiliation: Department of Microbiology and Immunology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232, United States.
authors.forename: Katherine L
authors.initials: KL
authors.lastname: Germane
authors.forename: Benjamin W
authors.initials: BW
authors.lastname: Spiller
mesh_terms: D001665:Binding Sites; D054308:Enteropathogenic Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D037521:Virulence Factors / Q000737:chemistry / Q000378:metabolism; D054462:p21-Activated Kinases / Q000737:chemistry* / Q000378:metabolism
chemical_list: D029968:Escherichia coli Proteins; C429282:EspG protein, E coli; D037521:Virulence Factors; D054462:p21-Activated Kinases