PT  - JOURNAL ARTICLE
AU  - Romão, Maria J.
AU  - Archer, Margarida
AU  - Moura, Isabel
AU  - Moura, José J. G.
AU  - LeGall, Jean
AU  - Engh, Richard
AU  - Schneider, Monika
AU  - Hof, Peter
AU  - Huber, Robert
TI  - Crystal Structure of the Xanthine Oxidase-Related Aldehyde Oxido-Reductase from <em>D. gigas</em>
AID  - 10.1126/science.270.5239.1170
DP  - 1995 Nov 17
TA  - Science
PG  - 1170--1176
VI  - 270
IP  - 5239
4099  - http://science.sciencemag.org/content/270/5239/1170.short
4100  - http://science.sciencemag.org/content/270/5239/1170.full
SO  - Science1995 Nov 17; 270
AB  - 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 Å 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.