4kf1

Crystal structure of SsoPox W263I in complex with C10HTL

spinqualitylabelsall models 4kf1, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4kf1 is a 4 chain structure with sequence from Atcc 35091. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CO, EDO, FE2, GOL, HT5, PG4 NonStd Res: KCX Related: 2vc5, 2vc7, 3uf9, 4ker, 4kes, 4ket, 4keu, 4kev, 4kez Gene: php, php SSO2522, SSO2522 (ATCC 35091) Activity: Aryldialkylphosphatase, with EC number 3.1.8.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PHP_SULSO] Has a low paraoxonase activity. Also active, but with a lower activity, against other oregano-phosphorus insecticides such as Dursban, Coumaphos, pNP-butanoate or parathion. Publication Abstract from PubMed Enzymes are proficient catalysts that enable fast rates of Michaelis-complex formation, the chemical step and products release. These different steps may require different conformational states of the active site that have distinct binding properties. Moreover, the conformational flexibility of the active site mediates alternative, promiscuous functions. Here we focused on the lactonase SsoPox from Sulfolobus solfataricus. SsoPox is a native lactonase endowed with promiscuous phosphotriesterase activity. We identified a position in the active site loop (W263) that governs its flexibility, and thereby affects the substrate specificity of the enzyme. We isolated two different sets of substitutions at position 263 that induce two distinct conformational sampling of the active loop and characterized the structural and kinetic effects of these substitutions. These sets of mutations selectively and distinctly mediate the improvement of the promiscuous phosphotriesterase and oxo-lactonase activities of SsoPox by increasing active-site loop flexibility. These observations corroborate the idea that conformational diversity governs enzymatic promiscuity and is a key feature of protein evolvability. Differential Active Site Loop Conformations Mediate Promiscuous Activities in the Lactonase SsoPox.,Hiblot J, Gotthard G, Elias M, Chabriere E PLoS One. 2013 Sep 23;8(9):e75272. doi: 10.1371/journal.pone.0075272. PMID:24086491 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphotriesterase 3D structures Serum Paraoxonase

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