Benjamin Spiller
Last active: 2/25/2021

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

Germane KL, Spiller BW
Biochemistry. 2011 50 (6): 917-9

PMID: 21235237 · PMCID: PMC3040069 · DOI:10.1021/bi1020138

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.

MeSH Terms (8)

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

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