SseA, a 3-mercaptopyruvate sulfurtransferase from escherichia coli : crystallization and preliminary crystallographic data
Articolo
Data di Pubblicazione:
2003
Citazione:
SseA, a 3-mercaptopyruvate sulfurtransferase from escherichia coli : crystallization and preliminary crystallographic data / A. Spallarossa, A. Carpen, F. Forlani, S. Pagani, M. Bolognesi, D. Bordo. - In: ACTA CRYSTALLOGRAPHICA. SECTION D, BIOLOGICAL CRYSTALLOGRAPHY. - ISSN 0907-4449. - 59:1(2003), pp. 168-170. [10.1107/S0907444902019248]
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 Angstrom. The in vivo role and substrate specificity of sulfurtransferase enzymes has been greatly debated. SseA, a 3-mecaptopyruvate: cyanide sulfurtransferase from E. coli, has been crystallized in a tetragonal crystal form suitable for X-ray crystallographic investigations.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
Clinical Biochemistry; Biochemistry, Genetics and Molecular Biology (all); Biochemistry; Biophysics; Condensed Matter Physics; Structural Biology
Elenco autori:
A. Spallarossa, A. Carpen, F. Forlani, S. Pagani, M. Bolognesi, D. Bordo
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