2IUK
Crystal structure of Soybean Lipoxygenase-D
2IUK の概要
| エントリーDOI | 10.2210/pdb2iuk/pdb |
| 分子名称 | SEED LIPOXYGENASE, FE (III) ION (3 entities in total) |
| 機能のキーワード | iron, dioxygenase, metal-binding, oxidoreductase, oxylipin biosynthesis, soybean lipoxygenase-d, fatty acid biosynthesis, lipid synthesis |
| 由来する生物種 | GLYCINE MAX (SOYBEAN) |
| 細胞内の位置 | Cytoplasm: P24095 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 193847.38 |
| 構造登録者 | Youn, B.,Sellhorn, G.E.,Mirchel, R.J.,Gaffney, B.J.,Grimes, H.D.,Kang, C. (登録日: 2006-06-05, 公開日: 2006-10-11, 最終更新日: 2024-06-19) |
| 主引用文献 | Youn, B.,Sellhorn, G.E.,Mirchel, R.J.,Gaffney, B.J.,Grimes, H.D.,Kang, C. Crystal Structures of Vegetative Soybean Lipoxygenase Vlx-B and Vlx-D, and Comparisons with Seed Isoforms Lox-1 and Lox-3. Proteins, 65:1008-, 2006 Cited by PubMed Abstract: 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. PubMed: 17022084DOI: 10.1002/PROT.21182 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.4 Å) |
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