6B6Y
Crystal structure of Desulfovibrio vulgaris carbon monoxide dehydrogenase, dithionite-reduced then oxygen-exposed (protein batch 2), oxidized C-cluster
Summary for 6B6Y
| Entry DOI | 10.2210/pdb6b6y/pdb |
| Descriptor | Carbon monoxide dehydrogenase, IRON/SULFUR CLUSTER, Fe(4)-Ni(1)-S(4) cluster, oxidized, ... (6 entities in total) |
| Functional Keywords | nickel-iron-sulfur (ni-fe-s) cluster, iron-sulfur (fe-s) cluster, metalloenzyme, oxidoreductase |
| Biological source | Desulfovibrio vulgaris |
| Total number of polymer chains | 2 |
| Total formula weight | 137223.66 |
| Authors | Wittenborn, E.C.,Drennan, C.L. (deposition date: 2017-10-03, release date: 2018-10-03, Last modification date: 2023-10-04) |
| Primary citation | Wittenborn, E.C.,Merrouch, M.,Ueda, C.,Fradale, L.,Leger, C.,Fourmond, V.,Pandelia, M.E.,Dementin, S.,Drennan, C.L. Redox-dependent rearrangements of the NiFeS cluster of carbon monoxide dehydrogenase. Elife, 7:-, 2018 Cited by PubMed Abstract: The C-cluster of the enzyme carbon monoxide dehydrogenase (CODH) is a structurally distinctive Ni-Fe-S cluster employed to catalyze the reduction of CO to CO as part of the Wood-Ljungdahl carbon fixation pathway. Using X-ray crystallography, we have observed unprecedented conformational dynamics in the C-cluster of the CODH from , providing the first view of an oxidized state of the cluster. Combined with supporting spectroscopic data, our structures reveal that this novel, oxidized cluster arrangement plays a role in avoiding irreversible oxidative degradation at the C-cluster. Furthermore, mutagenesis of a conserved cysteine residue that binds the C-cluster in the oxidized state but not in the reduced state suggests that the oxidized conformation could be important for proper cluster assembly, in particular Ni incorporation. Together, these results lay a foundation for future investigations of C-cluster activation and assembly, and contribute to an emerging paradigm of metallocluster plasticity. PubMed: 30277213DOI: 10.7554/eLife.39451 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
Download full validation report
