9HB9
A. vinelandii nitrogenase MoFe protein Anc1a
Summary for 9HB9
| Entry DOI | 10.2210/pdb9hb9/pdb |
| Related | 9HAZ |
| Descriptor | MoFe nitrogenase subunit D, Nitrogenase molybdenum-iron protein beta chain, iron-sulfur-molybdenum cluster with interstitial carbon, ... (7 entities in total) |
| Functional Keywords | nitrogen fixation, oxidoreductase |
| Biological source | Azotobacter vinelandii DJ More |
| Total number of polymer chains | 4 |
| Total formula weight | 236316.96 |
| Authors | Detemple, F.,Kacar, B.,Einsle, O. (deposition date: 2024-11-05, release date: 2025-09-10, Last modification date: 2025-10-01) |
| Primary citation | Cuevas Zuviria, B.,Detemple, F.,Amritkar, K.,Garcia, A.K.,Seefeldt, L.,Einsle, O.,Kacar, B. Structural evolution of nitrogenase over 3 billion years. Elife, 14:-, 2025 Cited by PubMed Abstract: Previously, we identified the only dinitrogen reduction mechanism known to date as an ancient feature conserved from nitrogenase ancestors, which we directly tested by resurrecting and integrating synthetic ancestral nitrogenases into the genome of (Garcia et al., 2023), a genetically tractable, nitrogen-fixing model bacterium. Here, we extend this paleomolecular approach to investigate the structural evolution of nitrogenase over billions of years of evolution by combining phylogenetics, ancestral sequence reconstruction, protein crystallography, and deep-learning based predictions. This study reveals that nitrogenase, while maintaining a conserved multimeric core, evolved novel modular features aligned with major environmental transitions, suggesting that subtle distal changes and transient regulatory adaptations were key to its long-term persistence and to shaping protein evolution over geologic time. The framework established here provides a foundation for identifying structural constraints that governed ancient proteins and for situating their sequences and structures within phylogenetic and environmental contexts across time. PubMed: 40934104DOI: 10.7554/eLife.105613 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.658 Å) |
Structure validation
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