Structural highlights
Publication Abstract from PubMed
NifEN plays an essential role in the biosynthesis of the nitrogenase iron-molybdenum (FeMo) cofactor (M cluster). It is an alpha(2)beta(2) tetramer that is homologous to the catalytic molybdenum-iron (MoFe) protein (NifDK) component of nitrogenase. NifEN serves as a scaffold for the conversion of an iron-only precursor to a matured form of the M cluster before delivering the latter to its target location within NifDK. Here, we present the structure of the precursor-bound NifEN of Azotobacter vinelandii at 2.6 angstrom resolution. From a structural comparison of NifEN with des-M-cluster NifDK and holo NifDK, we propose similar pathways of cluster insertion for the homologous NifEN and NifDK proteins.
Structure of precursor-bound NifEN: a nitrogenase FeMo cofactor maturase/insertase.,Kaiser JT, Hu Y, Wiig JA, Rees DC, Ribbe MW Science. 2011 Jan 7;331(6013):91-4. PMID:21212358[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kaiser JT, Hu Y, Wiig JA, Rees DC, Ribbe MW. Structure of precursor-bound NifEN: a nitrogenase FeMo cofactor maturase/insertase. Science. 2011 Jan 7;331(6013):91-4. PMID:21212358 doi:10.1126/science.1196954
