5tlq

Model structure of the oxidized PaDsbA1 and 3-[(2-methylbenzyl)sulfanyl]-4H-1,2,4-triazol-4-amine complex

spinqualitylabelsall models 5tlq Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5tlq is a 1 chain structure with sequence from Pseudomonas aeruginosa PAO1. This structure supersedes the now removed PDB entry 2mbu. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 1YO Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DSBA_PSEAE Involved in disulfide-bond formation. Acts by transferring its disulfide bond to other proteins (By similarity). Publication Abstract from PubMed At a time when the antibiotic drug discovery pipeline has stalled, antibiotic resistance is accelerating with catastrophic implications for our ability to treat bacterial infections. Globally we face the prospect of a future when common infections can once again kill. Anti-virulence approaches that target the capacity of the bacterium to cause disease rather than the growth or survival of the bacterium itself offer a tantalizing prospect of novel antimicrobials. They may also reduce the propensity to induce resistance by removing the strong selection pressure imparted by bactericidal or bacteriostatic agents. In the human pathogen Pseudomonas aeruginosa, disulfide bond protein A (PaDsbA1) plays a central role in the oxidative folding of virulence factors and is therefore an attractive target for the development of new anti-virulence antimicrobials. Using a fragment-based approach we have identified small molecules that bind to PaDsbA1. The fragment hits show selective binding to PaDsbA1 over the DsbA protein from Escherichia coli, suggesting that developing species-specific narrow-spectrum inhibitors of DsbA enzymes may be feasible. Structures of a co-complex of PaDsbA1 with the highest affinity fragment identified in the screen reveal that the fragment binds on the non-catalytic surface of the protein at a domain interface. This biophysical and structural data represent a starting point in the development of higher affinity compounds, which will be assessed for their potential as selective PaDsbA1 inhibitors. Fragment library screening identifies hits that bind to the non-catalytic surface of Pseudomonas aeruginosa DsbA1.,Mohanty B, Rimmer K, McMahon RM, Headey SJ, Vazirani M, Shouldice SR, Coincon M, Tay S, Morton CJ, Simpson JS, Martin JL, Scanlon MJ PLoS One. 2017 Mar 27;12(3):e0173436. doi: 10.1371/journal.pone.0173436., eCollection 2017. PMID:28346540 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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