9ONJ
L-cluster free apo-NifEN expressed in E. coli
Summary for 9ONJ
| Entry DOI | 10.2210/pdb9onj/pdb |
| EMDB information | 70642 |
| Descriptor | Nitrogenase iron-molybdenum cofactor biosynthesis protein NifE, Nitrogenase iron-molybdenum cofactor biosynthesis protein NifN (2 entities in total) |
| Functional Keywords | nitrogenase, complex, oxidoreductase |
| Biological source | Azotobacter vinelandii DJ More |
| Total number of polymer chains | 3 |
| Total formula weight | 151381.03 |
| Authors | Neumann, B.,Brandon, K.,Suder, D.S.,Hu, Y.,Ribbe, M.W.,Gonen, S. (deposition date: 2025-05-15, release date: 2026-02-18, Last modification date: 2026-09-02) |
| Primary citation | Neumann, B.,Brandon, K.A.,Quechol, R.,Suder, D.S.,Lee, C.C.,Yang, Y.,Gorecki, K.,Wiig, J.A.,Hu, Y.,Gonen, S.,Ribbe, M.W. Structural insights into metallocluster trafficking in the nitrogenase assembly scaffold NifEN. Nat Catal, 9:281-294, 2026 Cited by PubMed Abstract: Nitrogenase catalyses small-molecule activation, and has great relevance to agronomy, environment and energy. Understanding the assembly of the complex nitrogenase cofactor is a decades-long goal in the field, and structural insights into this process remain scarce. Here we report a cryogenic electron microscopy (cryo-EM) study of heterologously expressed NifEN, a key player converting the precursor (L-cluster) to a mature cofactor (M-cluster). Structural analyses of apo- and holo-NifEN demonstrate major conformational changes triggered by L-cluster incorporation. Further examinations of NifEN structures with inwardly and outwardly bound L-clusters, coupled with supporting mutational studies, AlphaFold 3 predictions and negative-stain EM analyses of NifEN complexed with upstream (NifB) and downstream (NifH) assembly partners, reveal a tunnel linking NifEN with NifB and NifH, with NifEN serving as a dynamic hub that coordinates L-cluster reception, maturation and delivery via conformation-gated metallocluster trafficking. PubMed: 41908675DOI: 10.1038/s41929-026-01489-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.72 Å) |
Structure validation
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