8UEM
The CryoEM structure of the high affinity Carbon monoxide dehydrogenase from Mycobacterium smegmatis
Summary for 8UEM
| Entry DOI | 10.2210/pdb8uem/pdb |
| Related | 8UDS |
| EMDB information | 42164 |
| Descriptor | Carbon monoxide dehydrogenase (Large chain), CoxL, Carbon monoxide dehydrogenase medium chain, [2Fe-2S] binding domain protein, ... (8 entities in total) |
| Functional Keywords | carbon monoxide dehydrogenase, mocu, mycobacterium smegmatis, high affinity, trace gas scavenging, oxidoreductase |
| Biological source | Mycolicibacterium smegmatis MC2 155 More |
| Total number of polymer chains | 6 |
| Total formula weight | 273749.43 |
| Authors | Grinter, R.,Venugopal, H.,Greening, C.,Gillett, D. (deposition date: 2023-10-02, release date: 2024-10-16, Last modification date: 2025-07-09) |
| Primary citation | Kropp, A.,Gillett, D.L.,Venugopal, H.,Gonzalvez, M.A.,Lingford, J.P.,Jain, S.,Barlow, C.K.,Zhang, J.,Greening, C.,Grinter, R. Quinone extraction drives atmospheric carbon monoxide oxidation in bacteria. Nat.Chem.Biol., 21:1058-1068, 2025 Cited by PubMed Abstract: Diverse bacteria and archaea use atmospheric CO as an energy source for long-term survival. Bacteria use [MoCu]-CO dehydrogenases (Mo-CODH) to convert atmospheric CO to carbon dioxide, transferring the obtained electrons to the aerobic respiratory chain. However, it is unknown how these enzymes oxidize CO at low concentrations and interact with the respiratory chain. Here, we use cryo-electron microscopy and structural modeling to show how Mo-CODH (CoxSML) from Mycobacterium smegmatis interacts with its partner, the membrane-bound menaquinone-binding protein CoxG. We provide electrochemical, biochemical and genetic evidence that Mo-CODH transfers CO-derived electrons to the aerobic respiratory chain through CoxG. Lastly, we show that Mo-CODH and CoxG genetically and structurally associate in diverse bacteria and archaea. These findings reveal the basis of the biogeochemically and ecologically important process of atmospheric CO oxidation, while demonstrating that long-range quinone transport is a general mechanism of energy conservation, which convergently evolved on multiple occasions. PubMed: 39881213DOI: 10.1038/s41589-025-01836-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (1.85 Å) |
Structure validation
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