3FG3

Crystal structure of Delta413-417:GS I805W LOX

3FG3 の概要

• エントリーDOI: 10.2210/pdb3fg3/pdb
• 関連するPDBエントリー: 2FNQ 3FG1 3FG4
• 分子名称: Allene oxide synthase-lipoxygenase protein, FE (II) ION, CALCIUM ION, ... (7 entities in total)
• 機能のキーワード: lipoxygenase, arichidonic metabolism, dioxygenase, fatty acid biosynthesis, heme, iron, lipid synthesis, lyase, membrane, metal-binding, multifunctional enzyme, oxidoreductase, oxylipin biosynthesis
• 由来する生物種: Plexaura homomalla (black sea rod)
• 細胞内の位置: Cytoplasm : O16025
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 322000.05

構造登録者

Neau, D.B.,Newcomer, M.E. (登録日: 2008-12-04, 公開日: 2009-08-18, 最終更新日: 2023-09-06)

主引用文献

Neau, D.B.,Gilbert, N.C.,Bartlett, S.G.,Boeglin, W.,Brash, A.R.,Newcomer, M.E.
The 1.85 A structure of an 8R-lipoxygenase suggests a general model for lipoxygenase product specificity.
Biochemistry, 48:7906-7915, 2009

PubMed Abstract: Lipoxygenases (LOX) play pivotal roles in the biosynthesis of leukotrienes and other biologically active eicosanoids derived from arachidonic acid. A mechanistic understanding of substrate recognition, when lipoxygenases that recognize the same substrate generate different products, can be used to help guide the design of enzyme-specific inhibitors. We report here the 1.85 A resolution structure of an 8R-lipoxygenase from Plexaura homomalla, an enzyme with a sequence approximately 40% identical to that of human 5-LOX. The structure reveals a U-shaped channel, defined by invariant amino acids, that would allow substrate access to the catalytic iron. We demonstrate that mutations within the channel significantly impact enzyme activity and propose a novel model for substrate binding potentially applicable to other members of this enzyme family.

PubMed: 19594169
DOI: 10.1021/bi900084m

実験手法

X-RAY DIFFRACTION (1.9 Å)