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TitleDynamics driving the precursor in NifEN scaffold during nitrogenase FeMo-cofactor assembly.
Journal, issue, pagesNat Chem Biol, Year 2025
Publish dateNov 14, 2025
AuthorsLucía Payá Tormo / Tu-Quynh Nguyen / Cameron Fyfe / Hind Basbous / Katarzyna Dobrzyńska / Carlos Echavarri-Erasun / Lydie Martin / Giorgio Caserta / Pierre Legrand / Andrea Thorn / Patricia Amara / Guy Schoehn / Mickaël V Cherrier / Luis M Rubio / Yvain Nicolet /
PubMed AbstractNitrogenase catalyzes atmospheric nitrogen fixation, a critical biological process that depends on an intricate organometallic cofactor assembled by a dedicated multiprotein system. Here we uncover ...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.
External linksNat Chem Biol / PubMed:41238839
MethodsEM (single particle) / X-ray diffraction
Resolution2.4 - 2.86 Å
Structure data

52557

9i0g

EMDB-52557, PDB-9i0g:
CryoEM structure of holo-GmNifEN
Method: EM (single particle) / Resolution: 2.86 Å

52558

9i0h

EMDB-52558, PDB-9i0h:
CryoEM structure of transit-GmNifEN
Method: EM (single particle) / Resolution: 2.62 Å

PDB-9i0f:
Revisited AvNifEN crystal structure
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-SF4:
IRON/SULFUR CLUSTER

ChemComp-S5Q:
FeFe cofactor

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-1PE:
PENTAETHYLENE GLYCOL / precipitant*YM

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-MG:
Unknown entry

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-HOH:
WATER

Source
  • geobacter metallireducens (bacteria)
  • azotobacter vinelandii dj (bacteria)
KeywordsMETAL BINDING PROTEIN / NITROGENASE COFACTOR MATURATION / PROTEIN BINDING / Metalloenzyme / Iron-Sulfur Cluster

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