3rde | pdb_00003rde

Crystal structure of the catalytic domain of porcine leukocyte 12-lipoxygenase

spinqualitylabelsall models 3rde, resolution 1.89Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3rde is a 4 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FE2, K, OYP Gene: ALOX12 (Sus scrofa) Activity: Arachidonate 12-lipoxygenase, with EC number 1.13.11.31 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Lipoxygenases are critical enzymes in the biosynthesis of families of bioactive lipids including compounds with important roles in the initiation and resolution of inflammation and in associated diseases such as diabetes, cardiovascular disease, and cancer. Crystals diffracting to high resolution (1.9 A) were obtained for a complex between the catalytic domain of leukocyte 12-lipoxygenase and the isoform-specific inhibitor, 4-(2-oxapentadeca-4-yne)phenylpropanoic acid (OPP). In the three-dimensional structure of the complex, the inhibitor occupied a new U-shaped channel open at one end to the surface of the protein and extending past the redox-active iron site that is essential for catalysis. In models, the channel accommodated arachidonic acid, defining the binding site for the substrate of the catalyzed reaction. There was a void adjacent to the OPP binding site connecting to the surface of the enzyme and providing a plausible access channel for the other substrate, oxygen. Crystal Structure of 12-Lipoxygenase Catalytic-Domain-Inhibitor Complex Identifies a Substrate-Binding Channel for Catalysis.,Xu S, Mueser TC, Marnett LJ, Funk MO Jr Structure. 2012 Jul 11. PMID:22795085 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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