5lir | pdb_00005lir

Structure of the SALTY Sigma cross-reacting protein 27A (SCRP-27A) from Salmonella typhimurium

spinqualitylabelsall models 5lir, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5lir is a 1 chain structure with sequence from "bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PEG NonStd Res: CSO Gene: yhbL, STM3327 ("Bacillus typhimurium" Loeffler 1892) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Gram-negative bacteria represent a challenging task for antibacterial drug discovery owing to their impermeable cell membrane and restricted uptake of small molecules. We herein describe the synthesis of natural-product-derived epoxycyclohexenones and explore their antibiotic activity against several pathogenic bacteria. A compound with activity against Salmonella Typhimurium was identified, and the target enzymes were unraveled by quantitative chemical proteomics. Importantly, two protein hits were linked to bacterial stress response, and corresponding assays revealed an elevated susceptibility to reactive oxygen species upon compound treatment. The consolidated inhibition of these targets provides a rationale for antibacterial activity and highlights epoxycyclohexenones as natural product scaffolds with suitable properties for killing Gram-negative Salmonella. Natural-Product-Inspired Aminoepoxybenzoquinones Kill Members of the Gram-Negative Pathogen Salmonella by Attenuating Cellular Stress Response.,Mandl FA, Kirsch VC, Ugur I, Kunold E, Vomacka J, Fetzer C, Schneider S, Richter K, Fuchs TM, Antes I, Sieber SA Angew Chem Int Ed Engl. 2016 Nov 14;55(47):14852-14857. doi:, 10.1002/anie.201607338. Epub 2016 Oct 26. PMID:27782347 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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