3RDE

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

3RDE の概要

• エントリーDOI: 10.2210/pdb3rde/pdb
• 分子名称: Arachidonate 12-lipoxygenase, 12S-type, POTASSIUM ION, FE (II) ION, ... (5 entities in total)
• 機能のキーワード: lipoxygenase, c-terminal domain, protein-inhibitor complex, 4-(2-oxapentadeca-4-yne)phenylpropanoic acid, lipoxygenase catalytic domain, dioxygenase, fe, leukocyte, oxidoreductase-oxidoreductase inhibitor complex, oxidoreductase/oxidoreductase inhibitor
• 由来する生物種: Sus scrofa (pigs,swine,wild boar)
• 細胞内の位置: Cytoplasm: P16469
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 260800.54

構造登録者

Funk, M.O.,Xu, S.,Marnett, L.J.,Mueser, T.C. (登録日: 2011-04-01, 公開日: 2012-04-18, 最終更新日: 2023-09-13)

主引用文献

Xu, S.,Mueser, T.C.,Marnett, L.J.,Funk, M.O.
Crystal structure of 12-lipoxygenase catalytic-domain-inhibitor complex identifies a substrate-binding channel for catalysis.
Structure, 20:1490-1497, 2012

PubMed Abstract: 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 Å) 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.

PubMed: 22795085
DOI: 10.1016/j.str.2012.06.003

実験手法

X-RAY DIFFRACTION (1.892 Å)