1OTJ

Crystal structure of APO (iron-free) TauD

1OTJ の概要

• エントリーDOI: 10.2210/pdb1otj/pdb
• 関連するPDBエントリー: 1OS7
• 分子名称: Alpha-Ketoglutarate-Dependent Taurine Dioxygenase, CHLORIDE ION, 2-AMINOETHANESULFONIC ACID, ... (4 entities in total)
• 機能のキーワード: jelly roll motif, alpha ketoglutarate-dependent dioxygenase, taurine, oxidoreductase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 130295.67

構造登録者

O'Brien, J.R.,Schuller, D.J.,Yang, V.S.,Dillard, B.D.,Lanzilotta, W.N. (登録日: 2003-03-21, 公開日: 2003-09-23, 最終更新日: 2024-02-14)

主引用文献

O'Brien, J.R.,Schuller, D.J.,Yang, V.S.,Dillard, B.D.,Lanzilotta, W.N.
Substrate-induced conformational changes in Escherichia coli taurine/alpha-ketoglutarate dioxygenase and insight into the oligomeric structure
Biochemistry, 42:5547-5554, 2003

PubMed Abstract: The enzymes in the alpha-ketoglutarate (alphaKG) dependent dioxygenase superfamily represent the largest class of non-heme iron oxidases and have important medical, ecological, and biotechnological roles. One such enzyme, taurine/alpha-ketoglutarate dioxygenase (TauD), catalyzes the conversion of 2-aminoethanesulfonate (taurine) to sulfite and aminoacetaldehyde while decomposing alphaKG to succinate and CO(2). This alphaKG dependent dioxygenase is expressed in Escherichia coli under sulfur starvation conditions and allows the cell to utilize taurine, and other similar sulfonates in the environment, as an alternative sulfur source. In this work, we report the structures of the apo and holo forms of TauD to 1.9 A resolution (R(cryst) = 21.2%, R(free) = 24.9%) and 2.5 A resolution (R(cryst) = 22.5%, R(free) = 27.8%), respectively. The models reported herein provide significant new insight into the substrate orientations at the active site and the conformational changes that are induced upon taurine binding. Furthermore, analysis of our crystallographic data coupled with reanalysis of the crystallographic model (resolution = 3.0 A, R(cryst) = 28.1, R(free) = 32.0) presented by Elkins et al. (Biochemistry (2002) 41, 5185-5192) reveals an alternative oligomeric arrangement for the enzyme that is consistent with the conserved primary and secondary structure elements of other alphaKG dependent dioxygenases.

PubMed: 12741810
DOI: 10.1021/bi0341096

実験手法

X-RAY DIFFRACTION (1.9 Å)