3S1L

Crystal Structure of Apo-form FurX

3S1L の概要

• エントリーDOI: 10.2210/pdb3s1l/pdb
• 関連するPDBエントリー: 3S2E 3S2F 3S2G 3S2I
• 分子名称: Zinc-containing alcohol dehydrogenase superfamily, ZINC ION, HEXAETHYLENE GLYCOL, ... (4 entities in total)
• 機能のキーワード: alcohol dehydrogenase, furfural, oxidoreductase
• 由来する生物種: Ralstonia eutropha (Alcaligenes eutrophus)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 144703.61

構造登録者

Hayes, R.,Sanchez, E.J.,Webb, B.N.,Hooper, T.,Nissen, M.S.,Li, Q.,Xun, L. (登録日: 2011-05-15, 公開日: 2012-04-25, 最終更新日: 2024-02-28)

主引用文献

Kang, C.,Hayes, R.,Sanchez, E.J.,Webb, B.N.,Li, Q.,Hooper, T.,Nissen, M.S.,Xun, L.
Furfural reduction mechanism of a zinc-dependent alcohol dehydrogenase from Cupriavidus necator JMP134.
Mol.Microbiol., 83:85-95, 2012

PubMed Abstract: FurX is a tetrameric Zn-dependent alcohol dehydrogenase (ADH) from Cupriavidus necator JMP134. The enzyme rapidly reduces furfural with NADH as the reducing power. For the first time among characterized ADHs, the high-resolution structures of all reaction steps were obtained in a time-resolved manner, thereby illustrating the complete catalytic events of NADH-dependent reduction of furfural and the dynamic Zn(2+) coordination among Glu66, water, substrate and product. In the fully closed conformation of the NADH complex, the catalytic turnover proved faster than observed for the partially closed conformation due to an effective proton transfer network. The domain motion triggered by NAD(H) association/dissociation appeared to facilitate dynamic interchanges in Zn(2+) coordination with substrate and product molecules, ultimately increasing the enzymatic turnover rate. NAD(+) dissociation appeared to be a slow process, involving multiple steps in concert with a domain opening and reconfiguration of Glu66. This agrees with the report that the cofactor is not dissociated from FurX during ethanol-dependent reduction of furfural, in which ethanol reduces NAD(+) to NADH that is subsequently used for furfural reduction.

PubMed: 22081946
DOI: 10.1111/j.1365-2958.2011.07914.x

実験手法

X-RAY DIFFRACTION (1.9 Å)