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

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


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

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


  • Escherichia coli Proteins
  • EspG protein, E coli
  • Virulence Factors
  • p21-Activated Kinases