3q1c | pdb_00003q1c

Structure of EspG Protein

spinqualitylabelsall models 3q1c, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3q1c is a 1 chain structure with sequence from Escherichia coli o127:h6. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: E2348C_3970, E2348_C_3970, espG (Escherichia coli O127:H6) Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. Structural and Functional Studies Indicate That the EPEC Effector, EspG, Directly Binds p21-Activated Kinase.,Germane KL, Spiller BW Biochemistry. 2011 Feb 15;50(6):917-9. Epub 2011 Jan 24. PMID:21235237 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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