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8CMW

A225L variant of the CODH/ACS complex of C. hydrogenoformans

8CMW の概要
エントリーDOI10.2210/pdb8cmw/pdb
分子名称Carbon monoxide dehydrogenase, NICKEL (II) ION, CO-methylating acetyl-CoA synthase, ... (11 entities in total)
機能のキーワードcodh, acs, oxidoreductase
由来する生物種Carboxydothermus hydrogenoformans Z-2901
詳細
タンパク質・核酸の鎖数2
化学式量合計156966.39
構造登録者
Ruickoldt, J.,Jeoung, J.,Lennartz, F.,Dobbek, H. (登録日: 2023-02-21, 公開日: 2024-03-06, 最終更新日: 2024-10-09)
主引用文献Ruickoldt, J.,Jeoung, J.H.,Rudolph, M.A.,Lennartz, F.,Kreibich, J.,Schomacker, R.,Dobbek, H.
Coupling CO 2 Reduction and Acetyl-CoA Formation: The Role of a CO Capturing Tunnel in Enzymatic Catalysis.
Angew.Chem.Int.Ed.Engl., 63:e202405120-e202405120, 2024
Cited by
PubMed Abstract: The bifunctional CO-dehydrogenase/acetyl-CoA synthase (CODH/ACS) complex couples the reduction of CO to the condensation of CO with a methyl moiety and CoA to acetyl-CoA. Catalysis occurs at two sites connected by a tunnel transporting the CO. In this study, we investigated how the bifunctional complex and its tunnel support catalysis using the CODH/ACS from Carboxydothermus hydrogenoformans as a model. Although CODH/ACS adapted to form a stable bifunctional complex with a secluded substrate tunnel, catalysis and CO transport is even more efficient when two monofunctional enzymes are coupled. Efficient CO channeling appears to be ensured by hydrophobic binding sites for CO, which act in a bucket-brigade fashion rather than as a simple tube. Tunnel remodeling showed that opening the tunnel increased activity but impaired directed transport of CO. Constricting the tunnel impaired activity and CO transport, suggesting that the tunnel evolved to sequester CO rather than to maximize turnover.
PubMed: 38743001
DOI: 10.1002/anie.202405120
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.6 Å)
構造検証レポート
Validation report summary of 8cmw
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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