3OWO

Structures of iron-dependent alcohol dehydrogenase 2 from Zymomonas mobilis ZM4 with and without NAD cofactor

3OWO の概要

• エントリーDOI: 10.2210/pdb3owo/pdb
• 関連するPDBエントリー: 3OX4
• 分子名称: Alcohol dehydrogenase 2, FE (II) ION (3 entities in total)
• 機能のキーワード: alcohol dehydrogenase 2, iron, oxidoreductase
• 由来する生物種: Zymomonas mobilis
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 160967.77

構造登録者

Moon, J.H.,Lee, H.J.,Song, J.M.,Park, S.Y.,Park, M.Y.,Park, H.M.,Sun, J.,Park, J.H.,Kim, J.S. (登録日: 2010-09-20, 公開日: 2011-02-16, 最終更新日: 2023-11-01)

主引用文献

Moon, J.H.,Lee, H.J.,Park, S.Y.,Song, J.M.,Park, M.Y.,Park, H.M.,Sun, J.,Park, J.H.,Kim, B.Y.,Kim, J.S.
Structures of iron-dependent alcohol dehydrogenase 2 from Zymomonas mobilis ZM4 with and without NAD+ cofactor
J.Mol.Biol., 407:413-424, 2011

PubMed Abstract: The ethanologenic bacterium Zymomonas mobilis ZM4 is of special interest because it has a high ethanol yield. This is made possible by the two alcohol dehydrogenases (ADHs) present in Z. mobilis ZM4 (zmADHs), which shift the equilibrium of the reaction toward the synthesis of ethanol. They are metal-dependent enzymes: zinc for zmADH1 and iron for zmADH2. However, zmADH2 is inactivated by oxygen, thus implicating zmADH2 as the component of the cytosolic respiratory system in Z. mobilis. Here, we show crystal structures of zmADH2 in the form of an apo-enzyme and an NAD+–cofactor complex. The overall folding of the monomeric structure is very similar to those of other functionally related ADHs with structural variations around the probable substrate and NAD+ cofactor binding region. A dimeric structure is formed by the limited interactions between the two subunits with the bound NAD+ at the cleft formed along the domain interface. The catalytic iron ion binds near to the nicotinamide ring of NAD+, which is likely to restrict and locate the ethanol to the active site together with the oxidized Cys residue and several nonpolar bulky residues. The structures of the zmADH2 from the proficient ethanologenic bacterium Z. mobilis, with and without NAD+ cofactor, and modeling ethanol in the active site imply that there is a typical metal-dependent catalytic mechanism.

PubMed: 21295587
DOI: 10.1016/j.jmb.2011.01.045

実験手法

X-RAY DIFFRACTION (2.07 Å)