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Purification, crystallization and preliminary X-ray diffraction analysis of adenosine triphosphate sulfurylase (ATPS) from the sulfate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774.
- Source :
-
Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2008 Jul 01; Vol. 64 (Pt 7), pp. 593-5. Date of Electronic Publication: 2008 Jun 07. - Publication Year :
- 2008
-
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.
- Subjects :
- Bacterial Proteins isolation & purification
Cobalt chemistry
Crystallization
Enzyme Activation physiology
Enzyme Stability
Sulfate Adenylyltransferase isolation & purification
Zinc chemistry
Bacterial Proteins chemistry
Desulfovibrio desulfuricans enzymology
Sulfate Adenylyltransferase chemistry
Sulfates chemistry
X-Ray Diffraction
Subjects
Details
- Language :
- English
- ISSN :
- 1744-3091
- Volume :
- 64
- Issue :
- Pt 7
- Database :
- MEDLINE
- Journal :
- Acta crystallographica. Section F, Structural biology and crystallization communications
- Publication Type :
- Academic Journal
- Accession number :
- 18607083
- Full Text :
- https://doi.org/10.1107/S1744309108008816