2iuk | pdb_00002iuk

Crystal structure of Soybean Lipoxygenase-D

spinqualitylabelsall models 2iuk, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2iuk is a 2 chain structure with sequence from Glycine hispida. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FE Activity: Oxidoreductase, with EC number 1.13.11.12 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [LOXX_SOYBN] Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. It catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The lipoxygenase family of lipid-peroxidizing, nonheme iron dioxygenases form products that are precursors for diverse physiological processes in both plants and animals. In soybean (Glycine max), five vegetative isoforms, VLX-A, VLX-B, VLX-C, VLX-D, VLX-E, and four seed isoforms LOX-1, LOX-2, LOX-3a, LOX-3b have been identified. In this study, we determined the crystal structures of the substrate-free forms of two major vegetative isoforms, with distinct enzymatic characteristics, VLX-B and VLX-D. Their structures are similar to the two seed isoforms, LOX-1 and LOX-3, having two domains with similar secondary structural elements: a beta-barrel N-terminal domain containing highly flexible loops and an alpha-helix-rich C-terminal catalytic domain. Detailed comparison of the structures of these two vegetative isoforms with the structures of LOX-1 and LOX-3 reveals important differences that help explain distinct aspects of the activity and positional specificity of these enzymes. In particular, the shape of the three branches of the internal subcavity, corresponding to substrate-binding and O(2) access, differs among the isoforms in a manner that reflects the differences in positional specificities. Crystal structures of vegetative soybean lipoxygenase VLX-B and VLX-D, and comparisons with seed isoforms LOX-1 and LOX-3.,Youn B, Sellhorn GE, Mirchel RJ, Gaffney BJ, Grimes HD, Kang C Proteins. 2006 Dec 1;65(4):1008-20. PMID:17022084 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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