9i0f | pdb_00009i0f

Revisited AvNifEN crystal structure

spinqualitylabelsall models 9i0f, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9i0f is a 8 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: X-ray diffraction, Resolution 2.4Å Ligands: 1PE, EDO, MG, PEG, PG4, PGE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C1DH03_AZOVD Publication Abstract from PubMed Nitrogenase catalyzes atmospheric nitrogen fixation, a critical biological process that depends on an intricate organometallic cofactor assembled by a dedicated multiprotein system. Here we uncover the structural basis for the function of NifEN, the scaffold protein that mediates the final stages of cofactor biosynthesis before its incorporation into nitrogenase. High-resolution structural analyses reveal that the cofactor precursor initially binds at a surface docking site before being transferred into a specialized cavity for further maturation. This process involves dynamic structural rearrangements, including coordinated domain motions and partial unfolding, enabling the scaffold to alternate between open and closed states. Additionally, a rear channel extends to the precursor-binding cavity, likely facilitating the entry of the modifying components molybdenum and homocitrate. These findings illuminate the dynamic mechanisms underlying FeMo-cofactor assembly and underscore the functional divergence between NifEN, the biosynthetic scaffold, and NifDK, the catalytic component of nitrogenase. Dynamics driving the precursor in NifEN scaffold during nitrogenase FeMo-cofactor assembly.,Paya Tormo L, Nguyen TQ, Fyfe C, Basbous H, Dobrzynska K, Echavarri-Erasun C, Martin L, Caserta G, Legrand P, Thorn A, Amara P, Schoehn G, Cherrier MV, Rubio LM, Nicolet Y Nat Chem Biol. 2025 Nov 14. doi: 10.1038/s41589-025-02070-4. PMID:41238839 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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