2iuk
From Proteopedia
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CRYSTAL STRUCTURE OF SOYBEAN LIPOXYGENASE-D
Overview
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 ... [(full description)]
About this Structure
2IUK is a [Single protein] structure of sequence from [Glycine max] with FE as [ligand]. Active as [[1]], with EC number [1.13.11.12]. Full crystallographic information is available from [OCA].
Reference
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
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