4le6

Crystal structure of the phosphotriesterase OPHC2 from Pseudomonas pseudoalcaligenes

spinqualitylabelsall models 4le6, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4le6 is a 5 chain structure with sequence from Pseudomonas oleovorans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: EDO, GOL, PGE, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5W503_PSEOL Publication Abstract from PubMed BACKGROUND: Organophosphates (OPs) are neurotoxic compounds for which current methods of elimination are unsatisfactory; thus bio-remediation is considered as a promising alternative. Here we provide the structural and enzymatic characterization of the recently identified enzyme isolated from Pseudomonas pseudoalcaligenes dubbed OPHC2. OPHC2 belongs to the metallo-beta-lactamase superfamily and exhibits an unusual thermal resistance and some OP degrading abilities. PRINCIPAL FINDINGS: The X-ray structure of OPHC2 has been solved at 2.1 A resolution. The enzyme is roughly globular exhibiting a alphabeta/betaalpha topology typical of the metallo-beta-lactamase superfamily. Several structural determinants, such as an extended dimerization surface and an intramolecular disulfide bridge, common features in thermostable enzymes, are consistent with its high Tm (97.8 degrees C). Additionally, we provide the enzymatic characterization of OPHC2 against a wide range of OPs, esters and lactones. SIGNIFICANCE: OPHC2 possesses a broad substrate activity spectrum, since it hydrolyzes various phosphotriesters, esters, and a lactone. Because of its organophosphorus hydrolase activity, and given its intrinsic thermostability, OPHC2 is an interesting candidate for the development of an OPs bio-decontaminant. Its X-ray structure shed light on its active site, and provides key information for the understanding of the substrate binding mode and catalysis. Structural and Enzymatic Characterization of the Phosphotriesterase OPHC2 from Pseudomonas pseudoalcaligenes.,Gotthard G, Hiblot J, Gonzalez D, Elias M, Chabriere E PLoS One. 2013 Nov 4;8(11):e77995. doi: 10.1371/journal.pone.0077995. PMID:24223749 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Phosphotriesterase 3D structures

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