5KAJ

Crystal structure of a dioxygenase in the Crotonase superfamily in P21, A319C mutant

5KAJ の概要

• エントリーDOI: 10.2210/pdb5kaj/pdb
• 関連するPDBエントリー: 5KAG 5KAH
• 分子名称: (3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase, [[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(3~{R})-4-[[3-[2-[(~{E})-2-[3,5-bis(oxidanyl)phenyl]-1-oxidanyl-ethenyl]sulfanylethylamino]-3-oxidanylidene-propyl]amino]-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-butyl] hydrogen phosphate (3 entities in total)
• 機能のキーワード: dioxygenase, dpgc, oxidoreductase
• 由来する生物種: Streptomyces toyocaensis
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 590290.33

構造登録者

Li, K.,Fielding, E.N.,Condurso, H.L.,Bruner, S.D. (登録日: 2016-06-01, 公開日: 2017-06-21, 最終更新日: 2023-09-27)

主引用文献

Li, K.,Fielding, E.N.,Condurso, H.L.,Bruner, S.D.
Probing the structural basis of oxygen binding in a cofactor-independent dioxygenase.
Acta Crystallogr D Struct Biol, 73:573-580, 2017

PubMed Abstract: The enzyme DpgC is included in the small family of cofactor-independent dioxygenases. The chemistry of DpgC is uncommon as the protein binds and utilizes dioxygen without the aid of a metal or organic cofactor. Previous structural and biochemical studies identified the substrate-binding mode and the components of the active site that are important in the catalytic mechanism. In addition, the results delineated a putative binding pocket and migration pathway for the co-substrate dioxygen. Here, structural biology is utilized, along with site-directed mutagenesis, to probe the assigned dioxygen-binding pocket. The key residues implicated in dioxygen trafficking were studied to probe the process of binding, activation and chemistry. The results support the proposed chemistry and provide insight into the general mechanism of dioxygen binding and activation.

PubMed: 28695857
DOI: 10.1107/S2059798317007045

実験手法

X-RAY DIFFRACTION (2.681 Å)