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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Binding Sites
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Enteropathogenic Escherichia coli / metabolism*
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Escherichia coli Proteins / chemistry*
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Escherichia coli Proteins / metabolism
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Models, Molecular
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Protein Conformation
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Structure-Activity Relationship
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Virulence Factors / chemistry
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Virulence Factors / metabolism
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p21-Activated Kinases / chemistry*
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p21-Activated Kinases / metabolism
Substances
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Escherichia coli Proteins
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EspG protein, E coli
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Virulence Factors
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p21-Activated Kinases