1OII
Crystal structure of the alkylsulfatase AtsK, a non-heme Fe(II) alphaketoglutarate dependent Dioxygenase in complex with iron and alphaketoglutarate
1OII の概要
エントリーDOI | 10.2210/pdb1oii/pdb |
関連するPDBエントリー | 1OIH 1OIJ 1OIK |
分子名称 | PUTATIVE ALKYLSULFATASE ATSK, FE (II) ION, 2-OXOGLUTARIC ACID, ... (4 entities in total) |
機能のキーワード | jelly roll, oxidoreductase |
由来する生物種 | PSEUDOMONAS PUTIDA |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 133801.38 |
構造登録者 | Mueller, I.,Kahnert, A.,Pape, T.,Dierks, T.,Meyer-Klauke, W.,Kertesz, M.A.,Uson, I. (登録日: 2003-06-18, 公開日: 2004-03-30, 最終更新日: 2023-12-13) |
主引用文献 | Mueller, I.,Kahnert, A.,Pape, T.,Sheldrick, G.M.,Meyer-Klaucke, W.,Dierks, T.,Kertesz, M.A.,Uson, I. Crystal Structure of the Alkylsulfatase Atsk: Insights Into the Catalytic Mechanism of the Fe(II) Alpha-Ketoglutarate-Dependent Dioxygenase Superfamily Biochemistry, 42:3075-, 2004 Cited by PubMed Abstract: The alkylsulfatase AtsK from Pseudomonas putida S-313 belongs to the widespread and versatile non-heme iron(II) alpha-ketoglutarate-dependent dioxygenase superfamily and catalyzes the oxygenolytic cleavage of a variety of different alkyl sulfate esters to the corresponding aldehyde and sulfate. The enzyme is only expressed under sulfur starvation conditions, providing a selective advantage for bacterial growth in soils and rhizosphere. Here we describe the crystal structure of AtsK in the apo form and in three complexes: with the cosubstrate alpha-ketoglutarate, with alpha-ketoglutarate and iron, and finally with alpha-ketoglutarate, iron, and an alkyl sulfate ester used as substrate in catalytic studies. The overall fold of the enzyme is closely related to that of the taurine/alpha-ketoglutarate dioxygenase TauD and is similar to the fold observed for other members of the enzyme superfamily. From comparison of these structures with the crystal structure of AtsK and its complexes, we propose a general mechanism for the catalytic cycle of the alpha-ketoglutarate-dependent dioxygenase superfamily. PubMed: 15023059DOI: 10.1021/BI035752V 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.19 Å) |
構造検証レポート
検証レポート(詳細版)をダウンロード