title: Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. gigas.
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.
authors.affiliation: Instituto de Tecnologia Química e Biológica, Oeiras, Portugal.
authors.forename: M J
authors.initials: MJ
authors.lastname: Romão
authors.forename: M
authors.initials: M
authors.lastname: Archer
authors.forename: I
authors.initials: I
authors.lastname: Moura
authors.forename: J J
authors.initials: JJ
authors.lastname: Moura
authors.forename: J
authors.initials: J
authors.lastname: LeGall
authors.forename: R
authors.initials: R
authors.lastname: Engh
authors.forename: M
authors.initials: M
authors.lastname: Schneider
authors.forename: P
authors.initials: P
authors.lastname: Hof
authors.forename: R
authors.initials: R
authors.lastname: Huber
mesh_terms: D000445:Aldehyde Oxidoreductases / Q000737:chemistry* / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D003067:Coenzymes / Q000737:chemistry / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D003597:Cytosine Nucleotides / Q000737:chemistry / Q000378:metabolism; D003901:Desulfovibrio / Q000201:enzymology*; D004331:Drosophila melanogaster / Q000201:enzymology; D004579:Electron Transport; D006860:Hydrogen Bonding; D007501:Iron / Q000737:chemistry; D008024:Ligands; D008667:Metalloproteins / Q000737:chemistry / Q000378:metabolism; D008969:Molecular Sequence Data; D008982:Molybdenum / Q000737:chemistry / Q000378:metabolism; D000090006:Molybdenum Cofactors; D010084:Oxidation-Reduction; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011621:Pteridines / Q000737:chemistry / Q000378:metabolism; D011622:Pterins / Q000737:chemistry / Q000378:metabolism; D019820:Xanthine; D014969:Xanthine Oxidase / Q000737:chemistry*; D014970:Xanthines / Q000378:metabolism
chemical_list: D000445:Aldehyde Oxidoreductases; D003067:Coenzymes; D003597:Cytosine Nucleotides; D007501:Iron; D008024:Ligands; D008667:Metalloproteins; D008982:Molybdenum; D000090006:Molybdenum Cofactors; D011621:Pteridines; D011622:Pterins; D019820:Xanthine; D014969:Xanthine Oxidase; D014970:Xanthines; C066895:molybdopterin cytosine dinucleotide; C022261:molybdopterin