Rees, D. C., Kim, J., Georgiadis, M. M., Komiya, H., Chirino, A. J., Woo, D., Schlessman, J., Chan, M. K., Joshua-Tor, L., Santillan, G., Chakrabarti, P., Hsu, B. T. (1993) Crystal Structures of the Iron Protein and Molybdenum-Iron Protein of Nitrogenase. In: Molybdenum Enzymes, Cofactors, and Model Systems. ACS Symposium Series, 535 (535). American Chemical Society, pp. 170-185. ISBN 0-8412-2708-X
Abstract
Three-dimensional structures of the nitrogenase iron protein and molybdenum-iron protein from Azotobacter vinelandii have been determined by x-ray crystallography. The iron protein contains a single 4Fe:4S cluster symmetrically liganded by two identical subunits. The molybdenum-iron protein is an α2?2 tetramer, where the homologous α and ? subunits surround two different types of metal centers: the FeMo-cofactor and the P-cluster pair. Both centers are constructed from two bridged clusters; the FeMo-cofactor has 4Fe:3S and 1Mo:3Fe:3S cluster bridged by three non-protein ligands, while the P-cluster pair contains two 4Fe:4S clusters bridged by two cysteine ligands located at the α? subunit interface. Docking studies between the iron protein and molybdenum iron protein suggest a possible interaction mode between these two proteins.
| Item Type: | Book Section |
|---|---|
| Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein structure rendering Investigative techniques and equipment > x ray crystallography |
| CSHL Authors: | |
| Communities: | CSHL labs > Joshua-Tor lab |
| Depositing User: | CSHL Librarian |
| Date: | 1993 |
| Date Deposited: | 20 Mar 2012 19:07 |
| Last Modified: | 17 Jan 2017 17:43 |
| URI: | https://repository.cshl.edu/id/eprint/25504 |
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