4mi7

Publication Abstract from PubMed

GtgE is an effector protein from Salmonella Typhimurium that modulates trafficking of the Salmonella-containing vacuole. It exerts its function by cleaving the Rab-family GTPases Rab29, Rab32 and Rab38, thereby preventing the delivery of antimicrobial factors to the bacteria-containing vacuole. Here, the crystal structure of GtgE at 1.65 A resolution is presented, and structure-based mutagenesis and in vivo infection assays are used to identify its catalytic triad. A panel of cysteine protease inhibitors were examined and it was determined that N-ethylmaleimide, antipain and chymostatin inhibit GtgE activity in vitro. These findings provide the basis for the development of novel therapeutic strategies to combat Salmonella infections.

Structural and enzymatic characterization of a host-specificity determinant from Salmonella.,Kohler AC, Spano S, Galan JE, Stebbins CE Acta Crystallogr D Biol Crystallogr. 2014 Feb;70(Pt 2):384-91. doi:, 10.1107/S1399004713028393. Epub 2014 Jan 29. PMID:24531472^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.