PMID:12571227
| Citation |
Rudolph, MJ, Wuebbens, MM, Turque, O, Rajagopalan, KV and Schindelin, H (2003) Structural studies of molybdopterin synthase provide insights into its catalytic mechanism. J. Biol. Chem. 278:14514-22 |
|---|---|
| Abstract |
Molybdenum cofactor biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea, and eukaryotes, including humans. Genetic deficiencies of enzymes involved in cofactor biosynthesis in humans lead to a severe and usually fatal disease. The molybdenum cofactor contains a tricyclic pyranopterin, termed molybdopterin, that bears the cis-dithiolene group responsible for molybdenum ligation. The dithiolene group of molybdopterin is generated by molybdopterin synthase, which consists of a large (MoaE) and small (MoaD) subunit. The crystal structure of molybdopterin synthase revealed a heterotetrameric enzyme in which the C terminus of each MoaD subunit is deeply inserted into a MoaE subunit to form the active site. In the activated form of the enzyme, the MoaD C terminus is present as a thiocarboxylate. The present study identified the position of the thiocarboxylate sulfur by exploiting the anomalous signal originating from the sulfur atom. The structure of molybdopterin synthase in a novel crystal form revealed a binding pocket for the terminal phosphate of molybdopterin, the product of the enzyme, and suggested a binding site for the pterin moiety present in precursor Z and molybdopterin. Finally, the crystal structure of the MoaE homodimer provides insights into the conformational changes accompanying binding of the MoaD subunit. |
| Links |
PubMed Online version:10.1074/jbc.M300449200 |
| Keywords |
Binding Sites; Catalysis; Dimerization; Escherichia coli/enzymology; Models, Chemical; Models, Molecular; Protein Binding; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Sulfur/chemistry; Sulfurtransferases/chemistry |
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