1LOX

RABBIT RETICULOCYTE 15-LIPOXYGENASE

1LOX の概要

• エントリーDOI: 10.2210/pdb1lox/pdb
• 分子名称: 15-LIPOXYGENASE, FE (II) ION, (2E)-3-(2-OCT-1-YN-1-YLPHENYL)ACRYLIC ACID, ... (4 entities in total)
• 機能のキーワード: oxidoreductase, 15lo_depot2
• 由来する生物種: Oryctolagus cuniculus (rabbit)
• 細胞内の位置: Cytoplasm, cytosol : P12530
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 75564.84

構造登録者

Gillmor, S.A.,Villasenor, A.,Fletterick, R.J.,Sigal, E.,Browner, M.F. (登録日: 1997-10-06, 公開日: 1998-11-04, 最終更新日: 2024-02-14)

主引用文献

Gillmor, S.A.,Villasenor, A.,Fletterick, R.,Sigal, E.,Browner, M.F.
The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity.
Nat.Struct.Biol., 4:1003-1009, 1997

PubMed Abstract: Here we report the first structure of a mammalian 15-lipoxygenase. The protein is composed of two domains; a catalytic domain and a previously unrecognized beta-barrel domain. The N-terminal beta-barrel domain has topological and sequence identify to a domain in the mammalian lipases, suggesting that these domains may have similar functions in vivo. Within the C-terminal domain, the lipoxygenase substrate binding site is a hydrophobic pocket defined by a bound inhibitor. Arachidonic acid can be docked into this deep hydrophobic pocket with the methyl end extending down into the bottom of the pocket and the acid end tethered by a conserved basic residue on the surface of the enzyme. This structure provides a unifying hypothesis for the positional specificity of mammalian lipoxygenases.

PubMed: 9406550
DOI: 10.1038/nsb1297-1003

実験手法

X-RAY DIFFRACTION (2.4 Å)