3h93 | pdb_00003h93

Crystal Structure of Pseudomonas aeruginosa DsbA

spinqualitylabelsall models 3h93, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3h93 is a 1 chain structure with sequence from Pseae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GOL NonStd Res: MSE Gene: dsbA, PA5489 (PSEAE) 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). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Bacterial antibiotic resistance is an emerging global crisis and treatment of multi-drug resistant Gram-negative infections, particularly those caused by the opportunistic human pathogen Pseudomonas aeruginosa, remains a major challenge. This problem is compounded by a lack of new antibiotics in the development pipeline: only two new classes have been developed since the 1960s and both are indicated for multi-drug resistant Gram-positive infections. A promising new approach to combat antibiotic resistance is by targeting bacterial virulence, rather than bacterial viability. The bacterial periplasmic protein DsbA represents a central point for anti-virulence intervention because its oxidoreductase activity is essential for the folding and function of almost all exported virulence factors. Here we describe the three-dimensional structure of this DsbA target from P. aeruginosa and we establish for the first time that a member of this enzyme family is capable of binding small molecules. We also describe biochemical assays that validate the redox activity of PaDsbA. Together the structural and functional characterization of PaDsbA provides the basis for future studies aimed at designing a new class of anti-virulence compounds to combat antibiotic-resistant P. aeruginosa infection. Characterisation of the DsbA oxidative folding catalyst from Pseudomonas aerugionsa reveals a highly oxidizing protein that binds small molecules.,Shouldice SR, Heras B, Jarrott R, Sharma P, Scanlon MJ, Martin J Antioxid Redox Signal. 2009 Sep 29. PMID:19788398 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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