PMID:12499560

Citation	Spallarossa, A, Carpen, A, Forlani, F, Pagani, S, Bolognesi, M and Bordo, D (2003) SseA, a 3-mercaptopyruvate sulfurtransferase from Escherichia coli: crystallization and preliminary crystallographic data. Acta Crystallogr. D Biol. Crystallogr. 59:168-70
Abstract	SseA, the translation product of the Escherichia coli sseA gene, is a 31 kDa protein endowed with 3-mercaptopyruvate:cyanide sulfurtransferase activity in vitro. As such, SseA is the prototype of a sulfurtransferase subfamily distinguished from the better known rhodanese sulfurtransferases, which display thiosulfate:cyanide sulfurtransferase activity. The physiological role of the two homologous enzyme families, whose catalytic activity is centred on a reactive invariant cysteine, is a matter of debate. In this framework, the forthcoming crystal structure analysis of SseA will be based on the tetragonal crystal form (space group P4(1) or P4(3)) reported here, with unit-cell parameters a = b = 150.2, c = 37.9 A.
Links	PubMed
Keywords	Amino Acid Sequence; Crystallization; Crystallography, X-Ray; Escherichia coli/enzymology; Molecular Sequence Data; Recombinant Proteins/biosynthesis; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Sequence Homology, Amino Acid; Sulfurtransferases/chemistry; Sulfurtransferases/genetics; Sulfurtransferases/metabolism; Thiosulfate Sulfurtransferase/chemistry; Thiosulfate Sulfurtransferase/genetics
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