| Literature DB >> 21212358 |
Jens T Kaiser1, Yilin Hu, Jared A Wiig, Douglas C Rees, Markus W Ribbe.
Abstract
NifEN plays an essential role in the biosynthesis of the nitrogenase iron-molybdenum (FeMo) cofactor (M cluster). It is an α(2)β(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.Entities:
Mesh:
Substances:
Year: 2011 PMID: 21212358 PMCID: PMC3138709 DOI: 10.1126/science.1196954
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728