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Please use this identifier to cite or link to this item: http://hdl.handle.net/10362/7027

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.
Texeira, Susana
Moura, José J. G.
Moura, Isabel
Romão, Maria J.
Trincão, José
Issue Date: 2008
Publisher: International Union of Crystallography
Abstract: 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.
Description: Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Jul 1;64(Pt 7):593-5
URI: http://hdl.handle.net/10362/7027
ISSN: 1744-3091
Appears in Collections:FCT: DQ - Artigos em revista internacional com arbitragem científica

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