8ahx

Cryo-EM structure of the nitrogen-fixation associated NADH:ferredoxin oxidoreductase RNF from Azotobacter vinelandii

spinqualitylabelsall models 8ahx, resolution 3.11Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8ahx is a 7 chain structure with sequence from Azotobacter vinelandii DJ. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.11Å Ligands: FES, FMN, LMT, RBF Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C1DMA8_AZOVD Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane.[HAMAP-Rule:MF_00459] Publication Abstract from PubMed Biological nitrogen fixation requires substantial metabolic energy in form of ATP as well as low-potential electrons that must derive from central metabolism. During aerobic growth, the free-living soil diazotroph Azotobacter vinelandii transfers electrons from the key metabolite NADH to the low-potential ferredoxin FdxA that serves as a direct electron donor to the dinitrogenase reductases. This process is mediated by the RNF complex that exploits the proton motive force over the cytoplasmic membrane to lower the midpoint potential of the transferred electron. Here we report the cryogenic electron microscopy structure of the nitrogenase-associated RNF complex of A. vinelandii, a seven-subunit membrane protein assembly that contains four flavin cofactors and six iron-sulfur centers. Its function requires the strict coupling of electron and proton transfer but also involves major conformational changes within the assembly that can be traced with a combination of electron microscopy and modeling. Architecture of the RNF1 complex that drives biological nitrogen fixation.,Zhang L, Einsle O Nat Chem Biol. 2024 Aug;20(8):1078-1085. doi: 10.1038/s41589-024-01641-1. Epub , 2024 Jun 18. PMID:38890433 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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