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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Aldehyde Oxidoreductases / chemistry*
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Aldehyde Oxidoreductases / metabolism
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Amino Acid Sequence
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Animals
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Coenzymes / chemistry
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Coenzymes / metabolism
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Crystallization
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Crystallography, X-Ray
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Cytosine Nucleotides / chemistry
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Cytosine Nucleotides / metabolism
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Desulfovibrio / enzymology*
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Drosophila melanogaster / enzymology
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Electron Transport
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Hydrogen Bonding
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Iron / chemistry
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Ligands
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Metalloproteins / chemistry
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Metalloproteins / metabolism
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Molecular Sequence Data
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Molybdenum / chemistry
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Molybdenum / metabolism
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Molybdenum Cofactors
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Oxidation-Reduction
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Protein Conformation
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Protein Folding
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Protein Structure, Secondary
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Pteridines / chemistry
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Pteridines / metabolism
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Pterins / chemistry
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Pterins / metabolism
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Xanthine
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Xanthine Oxidase / chemistry*
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Xanthines / metabolism
Substances
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Coenzymes
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Cytosine Nucleotides
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Ligands
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Metalloproteins
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Molybdenum Cofactors
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Pteridines
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Pterins
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Xanthines
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molybdopterin cytosine dinucleotide
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Xanthine
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Molybdenum
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molybdenum cofactor
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Iron
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Xanthine Oxidase
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Aldehyde Oxidoreductases