4TKU
Reactivated Nitrogenase MoFe-protein from A. vinelandii
Summary for 4TKU
| Entry DOI | 10.2210/pdb4tku/pdb |
| Related | 1M1N 3U7Q 4TKV |
| Descriptor | Nitrogenase molybdenum-iron protein alpha chain, Nitrogenase molybdenum-iron protein beta chain, 3-HYDROXY-3-CARBOXY-ADIPIC ACID, ... (9 entities in total) |
| Functional Keywords | nitrogenase, femo-cofactor, inhibition, oxidoreductase |
| Biological source | Azotobacter vinelandii More |
| Total number of polymer chains | 4 |
| Total formula weight | 233860.78 |
| Authors | Spatzal, T.,Perez, K.,Einsle, O.,Howard, J.B.,Rees, D.C. (deposition date: 2014-05-27, release date: 2014-10-01, Last modification date: 2023-12-27) |
| Primary citation | Spatzal, T.,Perez, K.A.,Einsle, O.,Howard, J.B.,Rees, D.C. Ligand binding to the FeMo-cofactor: structures of CO-bound and reactivated nitrogenase. Science, 345:1620-1623, 2014 Cited by PubMed Abstract: The mechanism of nitrogenase remains enigmatic, with a major unresolved issue concerning how inhibitors and substrates bind to the active site. We report a crystal structure of carbon monoxide (CO)-inhibited nitrogenase molybdenum-iron (MoFe)-protein at 1.50 angstrom resolution, which reveals a CO molecule bridging Fe2 and Fe6 of the FeMo-cofactor. The μ2 binding geometry is achieved by replacing a belt-sulfur atom (S2B) and highlights the generation of a reactive iron species uncovered by the displacement of sulfur. The CO inhibition is fully reversible as established by regain of enzyme activity and reappearance of S2B in the 1.43 angstrom resolution structure of the reactivated enzyme. The substantial and reversible reorganization of the FeMo-cofactor accompanying CO binding was unanticipated and provides insights into a catalytically competent state of nitrogenase. PubMed: 25258081DOI: 10.1126/science.1256679 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.43 Å) |
Structure validation
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