Open AccessPurification, crystallization and preliminary X‐ray diffraction analysis of adenosine triphosphate sulfurylase (ATPS) from the sulfate‐reducing bacterium Desulfovibrio desulfuricans ATCC 27774
Author(s) -
Gavel Olga Yu.,
Kladova Anna V.,
Bursakov Sergey A.,
Dias João M.,
Texeira Susana,
Shnyrov Valery L.,
Moura José J. G.,
Moura Isabel,
Romão Maria J.,
Trincão José
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108008816
Subject(s) - orthorhombic crystal system , chemistry , dimer , crystallization , zinc , bacteria , cobalt , enzyme , biochemistry , crystallography , inorganic chemistry , crystal structure , biology , organic chemistry , genetics
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.