3Q6J

Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M Oxidoreductase/Carboxylase

3Q6J の概要

• エントリーDOI: 10.2210/pdb3q6j/pdb
• 関連するPDBエントリー: 1MO9 1MOK 2C3D
• 分子名称: 2-oxopropyl-CoM reductase, carboxylating, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, FLAVIN-ADENINE DINUCLEOTIDE, ... (10 entities in total)
• 機能のキーワード: disulfide, carbon dioxide, coenzyme m, fad, nadp, oxidoreductase, carboxylase
• 由来する生物種: Xanthobacter autotrophicus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 118499.80

構造登録者

Pandey, A.S.,Mulder, D.W.,Ensign, S.A.,Peters, J.W. (登録日: 2011-01-01, 公開日: 2011-02-16, 最終更新日: 2023-09-13)

主引用文献

Pandey, A.S.,Mulder, D.W.,Ensign, S.A.,Peters, J.W.
Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M oxidoreductase/carboxylase.
Febs Lett., 585:459-464, 2011

PubMed Abstract: The structure of 2-ketopropyl coenzyme M oxidoreductase/carboxylase (2-KPCC) has been determined in a state in which CO(2) is observed providing insights into the mechanism of carboxylation. In the substrate encapsulated state of the enzyme, CO(2) is bound at the base of a narrow hydrophobic substrate access channel. The base of the channel is demarcated by a transition from a hydrophobic to hydrophilic environment where CO(2) is located in position for attack on the carbanion of the ketopropyl group of the substrate to ultimately produce acetoacetate. This binding mode effectively discriminates against H(2)O and prevents protonation of the ketopropyl leaving group.

PubMed: 21192936
DOI: 10.1016/j.febslet.2010.12.035

実験手法

X-RAY DIFFRACTION (1.92 Å)