8OIE
Iron Nitrogenase Complex from Rhodobacter capsulatus
Summary for 8OIE
| Entry DOI | 10.2210/pdb8oie/pdb |
| EMDB information | 16890 |
| Descriptor | Nitrogenase protein alpha chain, ALUMINUM FLUORIDE, IRON/SULFUR CLUSTER, ... (12 entities in total) |
| Functional Keywords | nitrogen fixation, fe nitrogenase, oxidoreductase |
| Biological source | Rhodobacter capsulatus SB 1003 More |
| Total number of polymer chains | 10 |
| Total formula weight | 375769.14 |
| Authors | Schmidt, F.V.,Schulz, L.,Zarzycki, J.,Prinz, S.,Erb, T.J.,Rebelein, J.G. (deposition date: 2023-03-22, release date: 2023-10-04, Last modification date: 2024-01-31) |
| Primary citation | Schmidt, F.V.,Schulz, L.,Zarzycki, J.,Prinz, S.,Oehlmann, N.N.,Erb, T.J.,Rebelein, J.G. Structural insights into the iron nitrogenase complex. Nat.Struct.Mol.Biol., 31:150-158, 2024 Cited by PubMed Abstract: Nitrogenases are best known for catalyzing the reduction of dinitrogen to ammonia at a complex metallic cofactor. Recently, nitrogenases were shown to reduce carbon dioxide (CO) and carbon monoxide to hydrocarbons, offering a pathway to recycle carbon waste into hydrocarbon products. Among the three nitrogenase isozymes, the iron nitrogenase has the highest wild-type activity for the reduction of CO, but the molecular architecture facilitating these activities has remained unknown. Here, we report a 2.35-Å cryogenic electron microscopy structure of the ADP·AlF-stabilized iron nitrogenase complex from Rhodobacter capsulatus, revealing an [FeSC-(R)-homocitrate] cluster in the active site. The enzyme complex suggests that the iron nitrogenase G subunit is involved in cluster stabilization and substrate channeling and confers specificity between nitrogenase reductase and catalytic component proteins. Moreover, the structure highlights a different interface between the two catalytic halves of the iron and the molybdenum nitrogenase, potentially influencing the intrasubunit 'communication' and thus the nitrogenase mechanism. PubMed: 38062208DOI: 10.1038/s41594-023-01124-2 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.35 Å) |
Structure validation
Download full validation report
