PMID:11080634

Citation	Stevenson, CE, Sargent, F, Buchanan, G, Palmer, T and Lawson, DM (2000) Crystal structure of the molybdenum cofactor biosynthesis protein MobA from Escherichia coli at near-atomic resolution. Structure 8:1115-25
Abstract	All mononuclear molybdoenzymes bind molybdenum in a complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This modification reaction is required for the functioning of many bacterial molybdoenzymes, including the nitrate reductases, dimethylsulfoxide (DMSO) and trimethylamine-N-oxide (TMAO) reductases, and formate dehydrogenases. The GMP attachment step is catalyzed by the cellular enzyme MobA.
Links	PubMed
Keywords	Amino Acid Sequence; Bacterial Proteins/chemistry; Binding Sites; Catalytic Domain; Coenzymes; Consensus Sequence; Crystallography, X-Ray; Escherichia coli/enzymology; Escherichia coli Proteins; Evolution, Molecular; Guanosine Monophosphate/metabolism; Metalloproteins/metabolism; Models, Molecular; Molecular Sequence Data; Protein Binding; Protein Conformation; Protein Structure, Secondary; Pteridines/metabolism; Recombinant Fusion Proteins/chemistry; Selenomethionine/chemistry; Sequence Alignment; Sequence Homology, Amino Acid
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