Crystal Structure of the Xanthine Oxidase-Related Aldehyde Oxido-Reductase from D. gigas

• Published in: Science (American Association for the Advancement of Science) 1995-11, Vol.270 (5239), p.1170-1176
• Main Authors: Romão, Maria J., Archer, Margarida, Moura, Isabel, Jose J. G. Moura, LeGall, Jean, Engh, Richard, Schneider, Monika, Hof, Peter, Huber, Robert
• Format: Article
• Language: English
• Subjects: Alcohol dehydrogenase; Alcohol dehydrogenases; Aldehyde Oxidoreductases - chemistry; Aldehyde Oxidoreductases - metabolism; Aldehydes; Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Animals; Atoms; Biological and medical sciences; Coenzymes - chemistry; Coenzymes - metabolism; Crystallization; Crystallography, X-Ray; Crystals; Cytosine Nucleotides - chemistry; Cytosine Nucleotides - metabolism; Desulfovibrio - enzymology; Desulfovibrio gigas; Drosophila melanogaster - enzymology; Electron Transport; Enzymes and enzyme inhibitors; Freshwater; Fundamental and applied biological sciences. Psychology; Hydrogen Bonding; Hydrogen bonds; Iron - chemistry; Ligands; Metalloproteins - chemistry; Metalloproteins - metabolism; Molecular Sequence Data; Molybdenum; Molybdenum - chemistry; Molybdenum - metabolism; Mops; Oxidases; Oxidation-Reduction; Oxidoreductases; Oxygen; Physiological aspects; Protein Conformation; Protein Folding; Protein structure; Protein Structure, Secondary; Proteins; Pteridines - chemistry; Pteridines - metabolism; Pterins - chemistry; Pterins - metabolism; Structure; Xanthine; Xanthine Oxidase - chemistry; Xanthines; Xanthines - metabolism
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.270.5239.1170

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 $\overset{circ}{\mathrm A}$ 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.