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Purification, crystallization and preliminary X-ray diffraction analysis of adenosine triphosphate sulfurylase (ATPS) from the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774
- Publication Year :
- 2008
- Publisher :
- International Union of Crystallography, 2008.
-
Abstract
- Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jul 1;64(Pt 7):593-5 Native zinc/cobalt-containing ATP sulfurylase (ATPS; EC 2.7.7.4; MgATP: sulfate adenylyltransferase) from Desulfovibrio desulfuricans ATCC 27774 was purified to homogeneity and crystallized. The orthorhombic crystals diffracted to beyond 2.5 A ° resolution and the X-ray data collected should allow the determination of the structure of the zinc-bound form of this ATPS. Although previous biochemical studies of this protein indicated the presence of a homotrimer in solution, a dimer was found in the asymmetric unit. Elucidation of this structure will permit a better understanding of the role of the metal in the activity and stability of this family of enzymes.
Details
- Language :
- English
- Database :
- OpenAIRE
- Accession number :
- edsair.od......1437..225ad6ec5089e4a307507ece583cc05b