Purification, crystallization and preliminary X-ray diffraction analysis of ade...

• Author(s): 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
• Date: 2008
• Persistent ID: http://hdl.handle.net/10362/7027
• Origin: Repositório Institucional da UNL
• Document Type: Article
• Language: English

Description

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.