3pi6 | pdb_00003pi6

Crystal structure of the CFTR inhibitory factor Cif with the H177Y mutation

spinqualitylabelsall models 3pi6, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3pi6 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 1.5Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H2ZD27_PSEAB Publication Abstract from PubMed The Gram-negative bacterium Pseudomonas aeruginosa is an opportunistic pathogen that secretes a multitude of virulence factors during the course of infection. Among these is Cif, an epoxide hydrolase (EH) that reduces the functional localization of the cystic fibrosis transmembrane conductance regulator in epithelial cells. In addition to being the first reported EH virulence factor, Cif possesses unique sequence deviations from canonical EH motifs. Foremost among these is the substitution of a histidine for the second epoxide ring-opening tyrosine in the active site. To test the functional equivalence of the Tyr and His side chains at this position, we have generated the mutant Cif-H177Y. Structural analysis confirms that both the WT His and mutant Tyr side chains can be accommodated without large-scale conformational changes. However, the Tyr mutation is functionally inactive. Based on a detailed analysis of the structure of the Tyr mutant, it appears that Cif's main-chain conformation imposes a functional requirement for a His at this position. Comparison with canonical EH structures reveals additional conformational differences, which are coupled to divergent sequence characteristics. When used to probe the genomes of other opportunistic pathogens, these sequence-structure criteria uncover candidate sequences that appear to form a distinct subfamily of Cif-like epoxide hydrolases characterized by a conserved His/Tyr ring-opening pair. Pseudomonas Aeruginosa Cif Defines a Distinct Class of alpha/beta Epoxide Hydrolases Utilizing a His/Tyr Ring-opening Pair.,Bahl CD, Madden DR Protein Pept Lett. 2011 Sep 20. PMID:21933119 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also CFTR inhibitory factor

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