9FZZ

Structure of carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS) in complex with corrinoid iron-sulfur protein (CoFeSP) from Clostridium autoethanogenum (composite structure, class 3B)

9FZZ の概要

• エントリーDOI: 10.2210/pdb9fzz/pdb
• EMDBエントリー: 50900
• 分子名称: CO-methylating acetyl-CoA synthase, Acetyl-CoA decarbonylase/synthase complex subunit delta, Carbon monoxide dehydrogenase/acetyl-CoA synthase beta subunit, ... (8 entities in total)
• 機能のキーワード: anaerobic co2 fixation, acetyl-coa synthesis, metalloenzyme, wood-ljungdahl pathway., oxidoreductase
• 由来する生物種: Clostridium autoethanogenum DSM 10061; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 377351.48

構造登録者

Yin, M.D.,Lemaire, O.N.,Wagner, T.,Murphy, B.J. (登録日: 2024-07-06, 公開日: 2025-02-05, 最終更新日: 2025-02-19)

主引用文献

Yin, M.D.,Lemaire, O.N.,Rosas Jimenez, J.G.,Belhamri, M.,Shevchenko, A.,Hummer, G.,Wagner, T.,Murphy, B.J.
Conformational dynamics of a multienzyme complex in anaerobic carbon fixation.
Science, 387:498-504, 2025

PubMed Abstract: In the ancient microbial Wood-Ljungdahl pathway, carbon dioxide (CO) is fixed in a multistep process that ends with acetyl-coenzyme A (acetyl-CoA) synthesis at the bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase complex (CODH/ACS). In this work, we present structural snapshots of the CODH/ACS from the gas-converting acetogen , characterizing the molecular choreography of the overall reaction, including electron transfer to the CODH for CO reduction, methyl transfer from the corrinoid iron-sulfur protein (CoFeSP) partner to the ACS active site, and acetyl-CoA production. Unlike CODH, the multidomain ACS undergoes large conformational changes to form an internal connection to the CODH active site, accommodate the CoFeSP for methyl transfer, and protect the reaction intermediates. Altogether, the structures allow us to draw a detailed reaction mechanism of this enzyme, which is crucial for CO fixation in anaerobic organisms.

PubMed: 39883773
DOI: 10.1126/science.adr9672

実験手法

ELECTRON MICROSCOPY (2.65 Å)