4wf5

Crystal structure of E.Coli DsbA soaked with compound 4

spinqualitylabelsall models 4wf5, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4wf5 is a 2 chain structure with sequence from Escherichia coli BL21(DE3). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.45Å Ligands: CU, EDO, GOL, WF4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H2UL03_ECOBD Publication Abstract from PubMed The thiol-disulfide oxidoreductase enzyme DsbA catalyzes the formation of disulfide bonds in the periplasm of Gram-negative bacteria. DsbA substrates include proteins involved in bacterial virulence. In the absence of DsbA, many of these proteins do not fold correctly, which renders the bacteria avirulent. Thus DsbA is a critical mediator of virulence and inhibitors may act as antivirulence agents. Biophysical screening has been employed to identify fragments that bind to DsbA from Escherichia coli. Elaboration of one of these fragments produced compounds that inhibit DsbA activity in vitro. In cell-based assays, the compounds inhibit bacterial motility, but have no effect on growth in liquid culture, which is consistent with selective inhibition of DsbA. Crystal structures of inhibitors bound to DsbA indicate that they bind adjacent to the active site. Together, the data suggest that DsbA may be amenable to the development of novel antibacterial compounds that act by inhibiting bacterial virulence. Application of Fragment-Based Screening to the Design of Inhibitors of Escherichia coli DsbA.,Adams LA, Sharma P, Mohanty B, Ilyichova OV, Mulcair MD, Williams ML, Gleeson EC, Totsika M, Doak BC, Caria S, Rimmer K, Horne J, Shouldice SR, Vazirani M, Headey SJ, Plumb BR, Martin JL, Heras B, Simpson JS, Scanlon MJ Angew Chem Int Ed Engl. 2014 Dec 30. doi: 10.1002/anie.201410341. PMID:25556635 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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