2E7Z

Acetylene Hydratase from Pelobacter acetylenicus

2E7Z の概要

• エントリーDOI: 10.2210/pdb2e7z/pdb
• 分子名称: Acetylene hydratase Ahy, SODIUM ION, ACETATE ION, ... (8 entities in total)
• 機能のキーワード: tungstoprotein, dmso reductase family, iron-sulfur-cluster, lyase
• 由来する生物種: Pelobacter acetylenicus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 83985.80

構造登録者

Einsle, O.,Kroneck, P.M.H.,Seiffert, G.B.,Messerschmidt, A. (登録日: 2007-01-15, 公開日: 2007-02-27, 最終更新日: 2024-12-25)

主引用文献

Seiffert, G.B.,Ullmann, G.M.,Messerschmidt, A.,Schink, B.,Kroneck, P.M.H.,Einsle, O.
Structure of the non-redox-active tungsten/[4Fe:4S] enzyme acetylene hydratase
Proc.Natl.Acad.Sci.Usa, 104:3073-3077, 2007

PubMed Abstract: The tungsten-iron-sulfur enzyme acetylene hydratase stands out from its class because it catalyzes a nonredox reaction, the hydration of acetylene to acetaldehyde. Sequence comparisons group the protein into the dimethyl sulfoxide reductase family, and it contains a bis-molybdopterin guanine dinucleotide-ligated tungsten atom and a cubane-type [4Fe:4S] cluster. The crystal structure of acetylene hydratase at 1.26 A now shows that the tungsten center binds a water molecule that is activated by an adjacent aspartate residue, enabling it to attack acetylene bound in a distinct, hydrophobic pocket. This mechanism requires a strong shift of pK(a) of the aspartate, caused by a nearby low-potential [4Fe:4S] cluster. To access this previously unrecognized W-Asp active site, the protein evolved a new substrate channel distant from where it is found in other molybdenum and tungsten enzymes.

PubMed: 17360611
DOI: 10.1073/pnas.0610407104

実験手法

X-RAY DIFFRACTION (1.26 Å)