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...

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Published inScience (American Association for the Advancement of Science) Vol. 331; no. 6013; pp. 91 - 94
Main Authors Kaiser, Jens T, Hu, Yilin, Wiig, Jared A, Rees, Douglas C, Ribbe, Markus W
Format Journal Article
LanguageEnglish
Published Washington, DC American Association for the Advancement of Science 07.01.2011
The American Association for the Advancement of Science
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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.
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These authors contributed equally to this work.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1196954