9FZY
Structure of carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS) in complex with corrinoid iron-sulfur protein (CoFeSP) from Clostridium autoethanogenum (composite structure, class 3A)
Summary for 9FZY
| Entry DOI | 10.2210/pdb9fzy/pdb |
| EMDB information | 50897 |
| Descriptor | Corrinoid iron-sulfur protein large subunit, CO-methylating acetyl-CoA synthase, Acetyl-CoA decarbonylase/synthase complex subunit delta, ... (8 entities in total) |
| Functional Keywords | anaerobic co2 fixation, acetyl-coa synthesis, metalloenzyme, wood-ljungdahl pathway., oxidoreductase |
| Biological source | Clostridium autoethanogenum DSM 10061 More |
| Total number of polymer chains | 6 |
| Total formula weight | 377351.48 |
| Authors | Yin, M.D.,Lemaire, O.N.,Wagner, T.,Murphy, B.J. (deposition date: 2024-07-06, release date: 2025-02-05, Last modification date: 2025-02-19) |
| Primary citation | 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 Cited by 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: 39883773DOI: 10.1126/science.adr9672 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.71 Å) |
Structure validation
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