Structural and Functional Studies Indicate That the EPEC Effector, EspG, Directly Binds p21-Activated Kinase
- Vanderbilt
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.
- Research Organization:
- Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Sponsoring Organization:
- OTHERNIH
- OSTI ID:
- 1023669
- Journal Information:
- Biochemistry-US, Vol. 60, Issue (6) ; 02, 2011; ISSN 0006-2960
- Country of Publication:
- United States
- Language:
- ENGLISH
Similar Records
Structurally Distinct Bacterial TBC-like GAPs Link Arf GTPase to Rab1 Inactivation to Counteract Host Defenses
Novel fold of VirA, a type III secretion system effector protein from Shigella flexneri
Structural and Functional Studies Indicate That Shigella VirA Is Not a Protease and Does Not Directly Destabilize Microtubules
Journal Article
·
Wed Oct 10 00:00:00 EDT 2012
· Cell
·
OSTI ID:1023669
+3 more
Novel fold of VirA, a type III secretion system effector protein from Shigella flexneri
Journal Article
·
Wed Jan 28 00:00:00 EST 2009
· Protein Sci.
·
OSTI ID:1023669
+4 more
Structural and Functional Studies Indicate That Shigella VirA Is Not a Protease and Does Not Directly Destabilize Microtubules
Journal Article
·
Mon Nov 24 00:00:00 EST 2008
· Biochemistry-US
·
OSTI ID:1023669
+1 more