4WZA
Asymmetric Nucleotide Binding in the Nitrogenase Complex
Summary for 4WZA
| Entry DOI | 10.2210/pdb4wza/pdb |
| Descriptor | Nitrogenase molybdenum-iron protein alpha chain, ADENOSINE-5'-DIPHOSPHATE, PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER, ... (12 entities in total) |
| Functional Keywords | nitrogenase, nucleotide binding, asymetry, complex, oxidoreductase |
| Biological source | Azotobacter vinelandii More |
| Total number of polymer chains | 8 |
| Total formula weight | 353029.55 |
| Authors | Tezcan, F.A.,Kaiser, J.T.,Howard, J.B.,Rees, D.C. (deposition date: 2014-11-19, release date: 2014-12-31, Last modification date: 2023-09-27) |
| Primary citation | Tezcan, F.A.,Kaiser, J.T.,Howard, J.B.,Rees, D.C. Structural evidence for asymmetrical nucleotide interactions in nitrogenase. J.Am.Chem.Soc., 137:146-149, 2015 Cited by PubMed Abstract: The roles of ATP hydrolysis in electron-transfer (ET) reactions of the nitrogenase catalytic cycle remain obscure. Here, we present a new structure of a nitrogenase complex crystallized with MgADP and MgAMPPCP, an ATP analogue. In this structure the two nucleotides are bound asymmetrically by the Fe-protein subunits connected to the two different MoFe-protein subunits. This binding mode suggests that ATP hydrolysis and phosphate release may proceed by a stepwise mechanism. Through the associated Fe-protein conformational changes, a stepwise mechanism is anticipated to prolong the lifetime of the Fe-protein-MoFe-protein complex and, in turn, could orchestrate the sequence of intracomplex ET required for substrate reduction. PubMed: 25522159DOI: 10.1021/ja511945e PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8995 Å) |
Structure validation
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