Purification, crystallization and preliminary X-ray diffraction analysis of adenosine triphosphate sulfurylase (ATPS) from the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774

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 Å resolution and the X-ray data collected should allow the...

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Bibliographic Details
Main Author: Gavel, Olga Yu (author)
Other Authors: Kladova, Anna V. (author), Bursakov, Sergey A. (author), Dias, João M. (author), Texeira, Susana (author), Shnyrov, Valery L. (author), Moura, José J. G. (author), Moura, Isabel (author), Romão, Maria J. (author), Trincão, José (author)
Format: article
Language:eng
Published: 2019
Subjects:
ATP sulfurylases
Cobalt
Sulfate-reducing bacteria
Zinc
Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics
Online Access:https://doi.org/10.1107/S1744309108008816
Country:Portugal
Oai:oai:run.unl.pt:10362/62998
Description
Summary: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 Å 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.

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