Structure of Precursor-Bound NifEN: A Nitrogenase FeMo Cofactor Maturase/Insertase
NifEN plays an essential role in the biosynthesis of the nitrogenase iron-molybdenum (FeMo) cofactor (M cluster). It is an α₂β₂ 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...
Saved in:
Published in | Science (American Association for the Advancement of Science) Vol. 331; no. 6013; pp. 91 - 94 |
---|---|
Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
Washington, DC
American Association for the Advancement of Science
07.01.2011
The American Association for the Advancement of Science |
Subjects | |
Online Access | Get full text |
Cover
Loading…
Summary: | NifEN plays an essential role in the biosynthesis of the nitrogenase iron-molybdenum (FeMo) cofactor (M cluster). It is an α₂β₂ 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. |
---|---|
Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 ObjectType-Article-2 ObjectType-Feature-1 These authors contributed equally to this work. |
ISSN: | 0036-8075 1095-9203 |
DOI: | 10.1126/science.1196954 |