2IGA

Structure of Homoprotocatechuate 2,3-Dioxygenase from B. fuscum in complex with reactive intermediates formed via in crystallo reaction with 4-nitrocatechol at low oxygen concentrations.

2IGA の概要

• エントリーDOI: 10.2210/pdb2iga/pdb
• 関連するPDBエントリー: 2IG9
• 分子名称: Homoprotocatechuate 2,3-dioxygenase, FE (II) ION, CHLORIDE ION, ... (10 entities in total)
• 機能のキーワード: oxygenase, extradiol, fe(ii), homoprotocatechuate, alkylperoxo intermediate, substrate-semiquinone, open-ring product, oxidoreductase
• 由来する生物種: Brevibacterium fuscum
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 169371.19

構造登録者

Kovaleva, E.G.,Lipscomb, J.D. (登録日: 2006-09-22, 公開日: 2007-04-24, 最終更新日: 2023-08-30)

主引用文献

Kovaleva, E.G.,Lipscomb, J.D.
Crystal structures of Fe2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates
Science, 316:453-457, 2007

PubMed Abstract: We report the structures of three intermediates in the O2 activation and insertion reactions of an extradiol ring-cleaving dioxygenase. A crystal of Fe2+-containing homoprotocatechuate 2,3-dioxygenase was soaked in the slow substrate 4-nitrocatechol in a low O2 atmosphere. The x-ray crystal structure shows that three different intermediates reside in different subunits of a single homotetrameric enzyme molecule. One of these is the key substrate-alkylperoxo-Fe2+ intermediate, which has been predicted, but not structurally characterized, in an oxygenase. The intermediates define the major chemical steps of the dioxygenase mechanism and point to a general mechanistic strategy for the diverse 2-His-1-carboxylate enzyme family.

PubMed: 17446402
DOI: 10.1126/science.1134697

実験手法

X-RAY DIFFRACTION (1.95 Å)