2FNQ

Insights from the X-ray crystal structure of coral 8R-lipoxygenase: calcium activation via A C2-like domain and a structural basis of product chirality

「1ZQ4」から置き換えられました

2FNQ の概要

• エントリーDOI: 10.2210/pdb2fnq/pdb
• 関連するPDBエントリー: 1u5u
• 分子名称: Allene oxide synthase-lipoxygenase protein, FE (II) ION, CALCIUM ION (3 entities in total)
• 機能のキーワード: beta-barrel, eicosanoid, fatty acid, c2-like domain, oxidoreductase
• 由来する生物種: Plexaura homomalla
• 細胞内の位置: Cytoplasm: O16025
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 160227.22

構造登録者

Oldham, M.L.,Brash, A.R.,Newcomer, M.E. (登録日: 2006-01-11, 公開日: 2006-02-28, 最終更新日: 2024-02-14)

主引用文献

Oldham, M.L.,Brash, A.R.,Newcomer, M.E.
Insights from the X-ray crystal structure of coral 8R-lipoxygenase: calcium activation via a C2-like domain and a structural basis of product chirality.
J.Biol.Chem., 280:39545-39552, 2005

PubMed Abstract: Lipoxygenases (LOXs) catalyze the regio- and stereospecific dioxygenation of polyunsaturated membrane-embedded fatty acids. We report here the 3.2 A resolution structure of 8R-LOX from the Caribbean sea whip coral Plexaura homomalla, a LOX isozyme with calcium dependence and the uncommon R chiral stereospecificity. Structural and spectroscopic analyses demonstrated calcium binding in a C2-like membrane-binding domain, illuminating the function of similar amino acids in calcium-activated mammalian 5-LOX, the key enzyme in the pathway to the pro-inflammatory leukotrienes. Mutation of Ca(2+)-ligating amino acids in 8R-LOX resulted not only in a diminished capacity to bind membranes, as monitored by fluorescence resonance energy transfer, but also in an associated loss of Ca(2+)-regulated enzyme activity. Moreover, a structural basis for R chiral specificity is also revealed; creation of a small oxygen pocket next to Gly(428) (Ala in all S-LOX isozymes) promoted C-8 oxygenation with R chirality on the activated fatty acid substrate.

PubMed: 16162493
DOI: 10.1074/jbc.M506675200

実験手法

X-RAY DIFFRACTION (3.2 Å)