Kim, Jongsun and Rees, D. C. (1992) Crystallographic Structure and Functional Implications of the Nitrogenase Molybdenum-Iron Protein from Azotobacter vinelandii. Nature, 360 (6404). pp. 553-560. ISSN 0028-0836. doi:10.1038/360553a0. https://resolver.caltech.edu/CaltechAUTHORS:20150128-164438686
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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.
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| Contact Email Address: | phoebe@caltech.edu | |||||||||
| 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). | |||||||||
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| Issue or Number: | 6404 | |||||||||
| DOI: | 10.1038/360553a0 | |||||||||
| Record Number: | CaltechAUTHORS:20150128-164438686 | |||||||||
| Persistent URL: | https://resolver.caltech.edu/CaltechAUTHORS:20150128-164438686 | |||||||||
| Usage Policy: | No commercial reproduction, distribution, display or performance rights in this work are provided. | |||||||||
| ID Code: | 54210 | |||||||||
| Collection: | CaltechAUTHORS | |||||||||
| Deposited By: | SWORD User | |||||||||
| Deposited On: | 08 Feb 2015 06:35 | |||||||||
| Last Modified: | 10 Nov 2021 20:30 |
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