5BVG
Selenium incorporated nitrogenase MoFe-protein (Av1-Se2B) from A. vinelandii
Summary for 5BVG
| Entry DOI | 10.2210/pdb5bvg/pdb |
| Related | 3U7Q |
| Descriptor | Nitrogenase molybdenum-iron protein alpha chain, Nitrogenase molybdenum-iron protein beta chain, 3-HYDROXY-3-CARBOXY-ADIPIC ACID, ... (10 entities in total) |
| Functional Keywords | nitrogenase, femo-cofactor, se-incorporation, oxidoreductase |
| Biological source | Azotobacter vinelandii More |
| Total number of polymer chains | 4 |
| Total formula weight | 234181.58 |
| Authors | Spatzal, T.,Perez, K.A.,Howard, J.B.,Rees, D.C. (deposition date: 2015-06-05, release date: 2015-12-30, Last modification date: 2023-09-27) |
| Primary citation | Spatzal, T.,Perez, K.A.,Howard, J.B.,Rees, D.C. Catalysis-dependent selenium incorporation and migration in the nitrogenase active site iron-molybdenum cofactor. Elife, 4:e11620-e11620, 2015 Cited by PubMed Abstract: Dinitrogen reduction in the biological nitrogen cycle is catalyzed by nitrogenase, a two-component metalloenzyme. Understanding of the transformation of the inert resting state of the active site FeMo-cofactor into an activated state capable of reducing dinitrogen remains elusive. Here we report the catalysis dependent, site-selective incorporation of selenium into the FeMo-cofactor from selenocyanate as a newly identified substrate and inhibitor. The 1.60 Å resolution structure reveals selenium occupying the S2B site of FeMo-cofactor in the Azotobacter vinelandii MoFe-protein, a position that was recently identified as the CO-binding site. The Se2B-labeled enzyme retains substrate reduction activity and marks the starting point for a crystallographic pulse-chase experiment of the active site during turnover. Through a series of crystal structures obtained at resolutions of 1.32-1.66 Å, including the CO-inhibited form of Av1-Se2B, the exchangeability of all three belt-sulfur sites is demonstrated, providing direct insights into unforeseen rearrangements of the metal center during catalysis. PubMed: 26673079DOI: 10.7554/eLife.11620 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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