Structure of a Cofactor-Deficient Nitrogenase MoFe Protein
Abstract
One of the most complex biosynthetic processes in metallobiochemistry is the assembly of nitrogenase, the key enzyme in biological nitrogen fixation. We describe here the crystal structure of an iron-molybdenum cofactor–deficient form of the nitrogenase MoFe protein, into which the cofactor is inserted in the final step of MoFe protein assembly. The MoFe protein folds as a heterotetramer containing two copies each of the homologous α and β subunits. In this structure, one of the three α subunit domains exhibits a substantially changed conformation, whereas the rest of the protein remains essentially unchanged. A predominantly positively charged funnel is revealed; this funnel is of sufficient size to accommodate insertion of the negatively charged cofactor.
Additional Information
© 2002 American Association for the Advancement of Science. 18 January 2002; accepted 12 March 2002. This work was supported by NIH (B.K.B, D.R.D., and D.C.R.) and by a Deutsche Forschungsgemeinschaft research fellowship (B.S.). The rotation camera facility at the Stanford Synchrotron Radiation Laboratory is supported by the U.S. Department of Energy and NIH. Coordinates have been deposited with the Protein Data Bank (accession code 1L5H). Dedicated to the memory of Barbara K. Burgess (1 January 1951 to 30 December 2001).Attached Files
Supplemental Material - 1070010s1a.mov
Supplemental Material - 1070010s1b.mov
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Additional details
- Eprint ID
- 51860
- DOI
- 10.1126/science.1070010
- Resolver ID
- CaltechAUTHORS:20141117-141452827
- Deutsche Forschungsgemeinschaft (DFG)
- Department of Energy (DOE)
- NIH
- Created
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2014-11-18Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field