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

被引：0
|
作者：
Gavel, Olga Yu. [1 ]
Kladova, Anna V. [1 ]
Bursakov, Sergey A. [1 ]
Dias, Joao M. [1 ]
Texeira, Susana [1 ]
Shnyrov, Valery L. [1 ]
Moura, Jose J. G. [1 ]
Moura, Isabel [1 ]
Romao, Maria J. [1 ]
Trincao, Jose [1 ]
机构：
[1] Univ Nova Lisboa, Fac Ciencias & Tecnol, Centro Quim Fina & Biotechnol, Dept Quim,REQUIMTE, P-2829516 Caparica, Portugal
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2008年 / 64卷
关键词：
D O I：
10.1107/S1744309108008816
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
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 angstrom 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.
引用
收藏
页码：593 / 595
页数：3
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