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Structural and enzymatic characterization of a host-specificity determinant from Salmonella.


ABSTRACT: 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?Å 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.

SUBMITTER: Kohler AC 

PROVIDER: S-EPMC3940199 | biostudies-literature | 2014 Feb

REPOSITORIES: biostudies-literature

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Structural and enzymatic characterization of a host-specificity determinant from Salmonella.

Kohler Amanda C AC   Spanò Stefania S   Galán Jorge E JE   Stebbins C Erec CE  

Acta crystallographica. Section D, Biological crystallography 20140129 Pt 2


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 Å resolution is presented, and structure-based mutagenesis and in vivo infection assays are used to identify its catalytic triad. A panel of cysteine protease i  ...[more]

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