Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas
- Citation:
- Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas, Romao, M. J., Archer M., Moura I., Moura J. J., Legall J., Engh R., Schneider M., Hof P., and Huber R. , Science, Nov 17, Volume 270, Number 5239, p.1170-6, (1995)
Abstract:
The crystal structure of the aldehyde oxido-reductase (Mop) from the sulfate reducing anaerobic Gram-negative bacterium Desulfovibrio gigas has been determined at 2.25 A resolution by multiple isomorphous replacement and refined. The protein, a homodimer of 907 amino acid residues subunits, is a member of the xanthine oxidase family. The protein contains a molybdopterin cofactor (Mo-co) and two different [2Fe-2S] centers. It is folded into four domains of which the first two bind the iron sulfur centers and the last two are involved in Mo-co binding. Mo-co is a molybdenum molybdopterin cytosine dinucleotide. Molybdopterin forms a tricyclic system with the pterin bicycle annealed to a pyran ring. The molybdopterin dinucleotide is deeply buried in the protein. The cis-dithiolene group of the pyran ring binds the molybdenum, which is coordinated by three more (oxygen) ligands.
Notes:
0036-8075 (Print)0036-8075 (Linking)Journal ArticleResearch Support, Non-U.S. Gov't
