4MI7
Crystal Structure of Salmonella Effector Protein GtgE
Summary for 4MI7
| Entry DOI | 10.2210/pdb4mi7/pdb |
| Descriptor | Bacteriophage encoded virulence factor, SULFATE ION (3 entities in total) |
| Functional Keywords | bacterial protein, toxin, hydrolase |
| Biological source | Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344 |
| Total number of polymer chains | 1 |
| Total formula weight | 16041.86 |
| Authors | Kohler, A.C.,Stebbins, C.E. (deposition date: 2013-08-30, release date: 2014-02-12, Last modification date: 2024-02-28) |
| Primary citation | Kohler, A.C.,Spano, S.,Galan, J.E.,Stebbins, C.E. Structural and enzymatic characterization of a host-specificity determinant from Salmonella. Acta Crystallogr.,Sect.D, 70:384-391, 2014 Cited by PubMed 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. PubMed: 24531472DOI: 10.1107/S1399004713028393 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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