2IND

Mn(II) Reconstituted Toluene/o-xylene Monooxygenase Hydroxylase X-ray Crystal Structure

2IND の概要

• エントリーDOI: 10.2210/pdb2ind/pdb
• 関連するPDBエントリー: 1T0Q
• 分子名称: Toluene, o-xylene monooxygenase oxygenase subunit, TouB protein, MANGANESE (II) ION, ... (6 entities in total)
• 機能のキーワード: manganese reconstitution, 4-helix bundle, carboxylate bridge, metalloenzyme, oxidoreductase
• 由来する生物種: Pseudomonas stutzeri; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 104653.24

構造登録者

McCormick, M.S.,Sazinsky, M.H.,Condon, K.L.,Lippard, S.J. (登録日: 2006-10-06, 公開日: 2006-12-05, 最終更新日: 2023-08-30)

主引用文献

McCormick, M.S.,Sazinsky, M.H.,Condon, K.L.,Lippard, S.J.
X-ray crystal structures of manganese(II)-reconstituted and native toluene/o-xylene monooxygenase hydroxylase reveal rotamer shifts in conserved residues and an enhanced view of the protein interior.
J.Am.Chem.Soc., 128:15108-15110, 2006

PubMed Abstract: We report the X-ray crystal structures of native and manganese(II)-reconstituted toluene/o-xylene monooxygenase hydroxylase (ToMOH) from Pseudomonas stutzeri OX1 to 1.85 and 2.20 A resolution, respectively. The structures reveal that reduction of the dimetallic active site is accompanied by a carboxylate shift and alteration of the coordination environment for dioxygen binding and activation. A rotamer shift in a strategically placed asparagine 202 accompanies dimetallic center reduction and is proposed to influence protein component interactions. This rotamer shift is conserved between ToMOH and the corresponding residue in methane monooxygenase hydroxylase (MMOH). Previously unidentified hydrophobic pockets similar to those present in MMOH are assigned.

PubMed: 17117860
DOI: 10.1021/ja064837r

実験手法

X-RAY DIFFRACTION (2.2 Å)