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- Title
SseA, a 3-mercaptopyruvate sulfurtransferase from Escherichia coli: crystallization and preliminary crystallographic data.
- Authors
Spallarossa, Andrea; Carpen, Aristodemo; Forlani, Fabio; Pagani, Silvia; Bolognesi, Martino; Bordo, Domenico
- 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.
- Publication
Acta crystallographica. Section D, Biological crystallography, 2003, Vol 59, Issue Pt 1, p168
- ISSN
0907-4449
- Publication type
Journal Article
- DOI
10.1107/s0907444902019248