8BTS
Nitrogenase MoFe protein from A. vinelandii alpha double mutant C45A/L158C
Summary for 8BTS
| Entry DOI | 10.2210/pdb8bts/pdb |
| Descriptor | Nitrogenase protein alpha chain, Nitrogenase molybdenum-iron protein beta chain, 3-HYDROXY-3-CARBOXY-ADIPIC ACID, ... (8 entities in total) |
| Functional Keywords | n2-fixation, nitrogenase, cooperativity, ammonia, hydrogen, metalloenzyme, femo-cofactor, p cluster, o2-sensitivity, oxidoreductase |
| Biological source | Azotobacter vinelandii DJ More |
| Total number of polymer chains | 8 |
| Total formula weight | 472792.53 |
| Authors | Wagner, T.,Maslac, N. (deposition date: 2022-11-29, release date: 2023-06-07, Last modification date: 2024-06-19) |
| Primary citation | Cadoux, C.,Ratcliff, D.,Maslac, N.,Gu, W.,Tsakoumagkos, I.,Hoogendoorn, S.,Wagner, T.,Milton, R.D. Nitrogen Fixation and Hydrogen Evolution by Sterically Encumbered Mo-Nitrogenase. Jacs Au, 3:1521-1533, 2023 Cited by PubMed Abstract: The substrate-reducing proteins of all nitrogenases (MoFe, VFe, and FeFe) are organized as αß(γ) multimers with two functional halves. While their dimeric organization could afford improved structural stability of nitrogenases , previous research has proposed both negative and positive cooperativity contributions with respect to enzymatic activity. Here, a 1.4 kDa peptide was covalently introduced in the proximity of the P cluster, corresponding to the Fe protein docking position. The Strep-tag carried by the added peptide simultaneously sterically inhibits electron delivery to the MoFe protein and allows the isolation of partially inhibited MoFe proteins (where the half-inhibited MoFe protein was targeted). We confirm that the partially functional MoFe protein retains its ability to reduce N to NH, with no significant difference in selectivity over obligatory/parasitic H formation. Our experiment concludes that wild-type nitrogenase exhibits negative cooperativity during the steady state regarding H and NH formation (under Ar or N), with one-half of the MoFe protein inhibiting turnover in the second half. This emphasizes the presence and importance of long-range (>95 Å) protein-protein communication in biological N fixation in . PubMed: 37234119DOI: 10.1021/jacsau.3c00165 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.03 Å) |
Structure validation
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