8ENN
Homocitrate-deficient nitrogenase MoFe-protein from Azotobacter vinelandii nifV knockout
8ENN の概要
エントリーDOI | 10.2210/pdb8enn/pdb |
EMDBエントリー | 28272 28273 28274 28275 |
分子名称 | Nitrogenase molybdenum-iron protein alpha chain, Nitrogenase molybdenum-iron protein beta chain, iron-sulfur-molybdenum cluster with interstitial carbon, ... (8 entities in total) |
機能のキーワード | nitrogenase, nitrogen fixation, reductase, mofe, oxidoreductase |
由来する生物種 | Azotobacter vinelandii DJ 詳細 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 231295.40 |
構造登録者 | |
主引用文献 | Warmack, R.A.,Maggiolo, A.O.,Orta, A.,Wenke, B.B.,Howard, J.B.,Rees, D.C. Structural consequences of turnover-induced homocitrate loss in nitrogenase. Nat Commun, 14:1091-1091, 2023 Cited by PubMed Abstract: Nitrogenase catalyzes the ATP-dependent reduction of dinitrogen to ammonia during the process of biological nitrogen fixation that is essential for sustaining life. The active site FeMo-cofactor contains a [7Fe:1Mo:9S:1C] metallocluster coordinated with an R-homocitrate (HCA) molecule. Here, we establish through single particle cryoEM and chemical analysis of two forms of the Azotobacter vinelandii MoFe-protein - a high pH turnover inactivated species and a ∆NifV variant that cannot synthesize HCA - that loss of HCA is coupled to α-subunit domain and FeMo-cofactor disordering, and formation of a histidine coordination site. We further find a population of the ∆NifV variant complexed to an endogenous protein identified through structural and proteomic approaches as the uncharacterized protein NafT. Recognition by endogenous NafT demonstrates the physiological relevance of the HCA-compromised form, perhaps for cofactor insertion or repair. Our results point towards a dynamic active site in which HCA plays a role in enabling nitrogenase catalysis by facilitating activation of the FeMo-cofactor from a relatively stable form to a state capable of reducing dinitrogen under ambient conditions. PubMed: 36841829DOI: 10.1038/s41467-023-36636-4 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (2.58 Å) |
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