3vf1 | pdb_00003vf1

Structure of a calcium-dependent 11R-lipoxygenase suggests a mechanism for Ca-regulation

spinqualitylabelsall models 3vf1, resolution 2.47Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3vf1 is a 2 chain structure with sequence from Gersemia fruticosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FE2, SUC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Lipoxygenases (LOXs) are a key part of several signaling pathways that lead to inflammation and cancer. Yet, the mechanisms of substrate binding and allosteric regulation by the various LOX isoforms remain speculative. Here we report the 2.47 A resolution crystal structure of the arachidonate 11R-LOX from Gersemia fruticosa which sheds new light on the mechanism of LOX catalysis. Our crystallographic and mutational studies suggest that the aliphatic tail of the fatty acid is bound in a hydrophobic pocket with two potential entrances. We speculate that LOXs share a common T-shaped substrate channel architecture that gives rise to the varying positional specificities. A general allosteric mechanism is proposed for transmitting the activity-inducing effect of calcium binding from the membrane-targeting PLAT (polycystin-1/lipoxygenase/alpha-toxin) domain to the active site via a conserved pi-cation bridge. Structure of a calcium-dependent 11R-lipoxygenase suggests a mechanism for Ca2+-regulation.,Eek P, Jarving R, Jarving I, Gilbert NC, Newcomer ME, Samel N J Biol Chem. 2012 May 9. PMID:22573333 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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