Published December 10, 1992
| public
Journal Article
Crystallographic Structure and Functional Implications of the Nitrogenase Molybdenum-Iron Protein from Azotobacter vinelandii
- Creators
- Kim, Jongsun
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Rees, D. C.
Abstract
The crystal structure of the nitrogenase molybdenum–iron protein from Azotobacter vinelandii has been determined at 2.7 Å resolution. The α- and β-subunits in this α_2β_2 tetramer have similar polypeptide folds. The FeMo-cofactor is completely encompassed by the α-subunit, whereas the P-cluster pair occurs at the interface between α- and β-subunits. Structural similarities are apparent between nitrogenase and other electron transfer systems, including hydrogenases and the photosynthetic reaction centre.
Additional Information
© 1992 Nature Publishing Group. Received 17 September; accepted 24 November 1992. We thank J. B. Howard, A. J. Chirino, B. T. Hsu, M. K. Chan, H. Kamiya, D. Woo, G. Santillan and D. Malerba for contributions to this project. This work was supported by the NSF, with instrumentation funded in part by the Beckman Institute and the Joseph Irvine Equipment fund. X-PLOR calculations were done on the CRAY-YMP at the San Diego Supercomputer Center, supported by the NSF. Coordinates will be deposited in the Brookhaven Protein Data Bank, and are available by E-mail (REES@CITRAY.CALTECH.EDU).Additional details
- Eprint ID
- 54210
- DOI
- 10.1038/360553a0
- Resolver ID
- CaltechAUTHORS:20150128-164438686
- NSF
- Caltech Beckman Institute
- Joseph Irvine Equipment Fund
- Created
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2015-02-08Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field