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|Title:||Purification, crystallization and preliminary X-ray diffraction analysis of adenosine triphosphate sulfurylase (ATPS) from the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774|
|Authors:||Gavel, Olga Yu.|
Kladova, Anna V.
Bursakov, Sergey A.
Dias, João M.
Moura, José J. G.
Romão, Maria J.
|Publisher:||International Union of Crystallography|
|Abstract:||Native zinc/cobalt-containing ATP sulfurylase (ATPS; EC 188.8.131.52; 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.|
|Description:||Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jul 1;64(Pt 7):593-5|
|Appears in Collections:||FCT: DQ - Artigos em revista internacional com arbitragem científica|
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