PMID:10903949

Citation	Wuebbens, MM, Liu, MT, Rajagopalan, K and Schindelin, H (2000) Insights into molybdenum cofactor deficiency provided by the crystal structure of the molybdenum cofactor biosynthesis protein MoaC. Structure 8:709-18
Abstract	The molybdenum cofactor (Moco) is an essential component of a large family of enzymes involved in important transformations in carbon, nitrogen and sulfur metabolism. The Moco biosynthetic pathway is evolutionarily conserved and found in archaea, eubacteria and eukaryotes. In humans, genetic deficiencies of enzymes involved in this pathway trigger an autosomal recessive and usually deadly disease with severe neurological symptoms. The MoaC protein, together with the MoaA protein, is involved in the first step of Moco biosynthesis.
Links	PubMed
Keywords	Amino Acid Sequence; Archaeal Proteins/chemistry; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/isolation & purification; Bacterial Proteins/physiology; Binding Sites; Coenzymes; Crystallography, X-Ray; Escherichia coli/enzymology; Escherichia coli Proteins; Evolution, Molecular; Ferredoxins/genetics; Genes; Humans; Metalloproteins/biosynthesis; Metalloproteins/deficiency; Metalloproteins/metabolism; Models, Molecular; Molecular Sequence Data; Multigene Family; Mutagenesis, Site-Directed; Plant Proteins/chemistry; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Pteridines/metabolism; Recombinant Fusion Proteins/chemistry; Sequence Alignment; Sequence Homology, Amino Acid; Species Specificity; Structure-Activity Relationship
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