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.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
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.
|
| skos:exactMatch | |
| uniprot:name |
Biochemistry
|
| uniprot:author |
Germane K.L.,
Spiller B.W.
|
| uniprot:date |
2011
|
| uniprot:pages |
917-919
|
| uniprot:title |
Structural and functional studies indicate that the EPEC effector, EspG, directly binds p21-activated kinase.
|
| uniprot:volume |
50
|
| dc-term:identifier |
doi:10.1021/bi1020138
|