1N2C
NITROGENASE COMPLEX FROM AZOTOBACTER VINELANDII STABILIZED BY ADP-TETRAFLUOROALUMINATE
Summary for 1N2C
| Entry DOI | 10.2210/pdb1n2c/pdb |
| Descriptor | NITROGENASE MOLYBDENUM-IRON PROTEIN, ADENOSINE-5'-DIPHOSPHATE, IRON/SULFUR CLUSTER, ... (11 entities in total) |
| Functional Keywords | nitrogenase, nitrogen fixation, signal transduction, electron transfer, atp hydrolysis, complex of nitrogenase proteins |
| Biological source | Azotobacter vinelandii More |
| Total number of polymer chains | 8 |
| Total formula weight | 361248.21 |
| Authors | Schindelin, H.,Kisker, C.,Rees, D.C. (deposition date: 1997-05-02, release date: 1997-11-12, Last modification date: 2024-05-22) |
| Primary citation | Schindelin, H.,Kisker, C.,Schlessman, J.L.,Howard, J.B.,Rees, D.C. Structure of ADP x AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction. Nature, 387:370-376, 1997 Cited by PubMed Abstract: The coupling of ATP hydrolysis to electron transfer by the enzyme nitrogenase during biological nitrogen fixation is an important example of a nucleotide-dependent transduction mechanism. The crystal structure has been determined for the complex between the Fe-protein and MoFe-protein components of nitrogenase stabilized by ADP x AIF4-, previously used as a nucleoside triphosphate analogue in nucleotide-switch proteins. The structure reveals that the dimeric Fe-protein has undergone substantial conformational changes. The beta-phosphate and AIF4- groups are stabilized through intersubunit contacts that are critical for catalysis and the redox centre is repositioned to facilitate electron transfer. Interactions in the nitrogenase complex have broad implications for signal and energy transduction mechanisms in multiprotein complexes. PubMed: 9163420DOI: 10.1038/387370a0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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