7UT9
CryoEM structure of Azotobacter vinelandii nitrogenase complex (1:1 FeP:MoFeP, ADP/ATP-bound) during catalytic N2 reduction
Summary for 7UT9
| Entry DOI | 10.2210/pdb7ut9/pdb |
| EMDB information | 26763 |
| Descriptor | Nitrogenase molybdenum-iron protein alpha chain, IRON/SULFUR CLUSTER, ADENOSINE-5'-TRIPHOSPHATE, ... (12 entities in total) |
| Functional Keywords | nitrogenase, mofep, nitrogen fixation, fep, oxidoreductase |
| Biological source | Azotobacter vinelandii DJ More |
| Total number of polymer chains | 6 |
| Total formula weight | 297670.28 |
| Authors | Rutledge, H.L.,Cook, B.,Tezcan, F.A.,Herzik, M.A. (deposition date: 2022-04-26, release date: 2022-08-17, Last modification date: 2024-02-14) |
| Primary citation | Rutledge, H.L.,Cook, B.D.,Nguyen, H.P.M.,Herzik Jr., M.A.,Tezcan, F.A. Structures of the nitrogenase complex prepared under catalytic turnover conditions. Science, 377:865-869, 2022 Cited by PubMed Abstract: The enzyme nitrogenase couples adenosine triphosphate (ATP) hydrolysis to the multielectron reduction of atmospheric dinitrogen into ammonia. Despite extensive research, the mechanistic details of ATP-dependent energy transduction and dinitrogen reduction by nitrogenase are not well understood, requiring new strategies to monitor its structural dynamics during catalytic action. Here, we report cryo-electron microscopy structures of the nitrogenase complex prepared under enzymatic turnover conditions. We observe that asymmetry governs all aspects of the nitrogenase mechanism, including ATP hydrolysis, protein-protein interactions, and catalysis. Conformational changes near the catalytic iron-molybdenum cofactor are correlated with the nucleotide-hydrolysis state of the enzyme. PubMed: 35901182DOI: 10.1126/science.abq7641 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.44 Å) |
Structure validation
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