Structure of Precursor-Bound NifEN: A Nitrogenase FeMo Cofactor Maturase/Insertase

Creators: Kaiser, Jens T.; Hu, Yilin; Wiig, Jared A.; Rees, Douglas C.; Ribbe, Markus W.

Abstract

NifEN plays an essential role in the biosynthesis of the nitrogenase iron-molybdenum (FeMo) cofactor (M cluster). It is an α_2β_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.

Additional Information

© 2011 American Association for the Advancement of Science. Received for publication 25 August 2010. Accepted for publication 5 November 2010. This work was supported by NIH grants GM-67626 (M.W.R.) and GM-45162 (D.C.R.) D.C.R. is an investigator of the Howard Hughes Medical Institute. We acknowledge the Gordon and Betty Moore Foundation for support of the Molecular Observatory at California Institute of Technology. Operations at the Stanford Synchrotron Radiation Lightsource are supported by the U.S. Department of Energy and NIH. The coordinates and structure factors have been deposited with the Protein Data Bank (PDB), accession number 3PDI.

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