Unknown

Dataset Information

0

Structure of precursor-bound NifEN: a nitrogenase FeMo cofactor maturase/insertase.


ABSTRACT: NifEN plays an essential role in the biosynthesis of the nitrogenase iron-molybdenum (FeMo) cofactor (M cluster). It is an ?(2)?(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.

SUBMITTER: Kaiser JT 

PROVIDER: S-EPMC3138709 | biostudies-literature | 2011 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

Structure of precursor-bound NifEN: a nitrogenase FeMo cofactor maturase/insertase.

Kaiser Jens T JT   Hu Yilin Y   Wiig Jared A JA   Rees Douglas C DC   Ribbe Markus W MW  

Science (New York, N.Y.) 20110101 6013


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  ...[more]

Similar Datasets

| S-EPMC1859895 | biostudies-other
| S-EPMC3102359 | biostudies-other
| S-EPMC4205161 | biostudies-literature
| S-EPMC5715403 | biostudies-literature
| S-EPMC3268367 | biostudies-literature
| S-EPMC3105220 | biostudies-literature
| S-EPMC3799348 | biostudies-literature