@article {2504,
	title = {Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas},
	journal = {Science},
	volume = {270},
	number = {5239},
	year = {1995},
	note = {<p>0036-8075 (Print)0036-8075 (Linking)Journal ArticleResearch Support, Non-U.S. Gov{\textquoteright}t</p>
},
	month = {Nov 17},
	pages = {1170-6},
	abstract = {<p>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.</p>
},
	keywords = {Aldehyde Oxidoreductases/*chemistry/metabolism, Amino Acid Sequence, Animals, Coenzymes/chemistry/metabolism, Crystallization, Crystallography, X-Ray, Cytosine Nucleotides/chemistry/metabolism, Desulfovibrio/*enzymology, Drosophila melanogaster/enzymology, Electron Transport, Hydrogen Bonding, Iron/chemistry, Ligands, Metalloproteins/chemistry/metabolism, Molecular Sequence Data, Molybdenum/chemistry/metabolism, Oxidation-Reduction, Protein Conformation, Protein Folding, Protein Structure, Secondary, Pteridines/chemistry/metabolism, Pterins/chemistry/metabolism, Xanthine, Xanthine Oxidase/*chemistry, Xanthines/metabolism},
	url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=PubMed\&dopt=Citation\&list_uids=7502041 },
	author = {Romao, M. J. and Archer, M. and Moura, I. and Moura, J. J. and Legall, J. and Engh, R. and Schneider, M. and Hof, P. and Huber, R.}
}
