5tnj | pdb_00005tnj

Crystal structure of the E153Q mutant of the CFTR inhibitory factor Cif containing the adducted 4-Vinyl-1-cyclohexene 1,2-epoxide hydrolysis intermediate

spinqualitylabelsall models 5tnj, resolution 1.65Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5tnj is a 4 chain structure with sequence from Pseudomonas aeruginosa UCBPP-PA14. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.65Å Ligands: 8MD, AVH, BVH, DVH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H2ZD27_PSEAB Publication Abstract from PubMed Pseudomonas aeruginosa secretes an epoxide hydrolase with catalytic activity that triggers degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) and perturbs other host defense networks. Targets of this CFTR inhibitory factor (Cif) are largely unknown, but include an epoxy-fatty acid. In this class of signaling molecules, chirality can be an important determinant of physiological output and potency. Here we explore the active-site chemistry of this two-step alpha/beta-hydrolase and its implications for an emerging class of virulence enzymes. In combination with hydrolysis data, crystal structures of 15 trapped hydroxyalkyl-enzyme intermediates reveal the stereochemical basis of Cif's substrate specificity, as well as its regioisomeric and enantiomeric preferences. The structures also reveal distinct sets of conformational changes that enable the active site to expand dramatically in two directions, accommodating a surprising array of potential physiological epoxide targets. These new substrates may contribute to Cif's diverse effects in vivo, and thus to the success of P. aeruginosa and other pathogens during infection. Active-Site Flexibility and Substrate Specificity in a Bacterial Virulence Factor: Crystallographic Snapshots of an Epoxide Hydrolase.,Hvorecny KL, Bahl CD, Kitamura S, Lee KSS, Hammock BD, Morisseau C, Madden DR Structure. 2017 May 2;25(5):697-707.e4. doi: 10.1016/j.str.2017.03.002. Epub 2017, Apr 6. PMID:28392259 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also CFTR inhibitory factor

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