7UTA

CryoEM structure of Azotobacter vinelandii nitrogenase complex (2:1 FeP:MoFeP) inhibited by BeFx during catalytic N2 reduction

Summary for 7UTA

• Entry DOI: 10.2210/pdb7uta/pdb
• EMDB information: 26764
• Descriptor: Nitrogenase molybdenum-iron protein alpha chain, ADENOSINE-5'-DIPHOSPHATE, BERYLLIUM, ... (12 entities in total)
• Functional Keywords: nitrogenase, mofep, nitrogen fixation, oxidoreductase
• Biological source: Azotobacter vinelandii DJ; More
• Total number of polymer chains: 8
• Total formula weight: 361977.48

Authors

Rutledge, H.L.,Cook, B.D.,Nguyen, H.P.M.,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

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: 35901182
DOI: 10.1126/science.abq7641

Experimental method

ELECTRON MICROSCOPY (2.4 Å)