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 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.
Gavel
Olga Yu
OY
REQUIMTE, Departamento de Química, Centro de Química Fina e Biotecnologia, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, 2829-516 Caparica, Portugal.
Kladova
Anna V
AV
Bursakov
Sergey A
SA
Dias
João M
JM
Texeira
Susana
S
Shnyrov
Valery L
VL
Moura
José J G
JJ
Moura
Isabel
I
Romão
Maria J
MJ
Trincão
José
J
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D003035:Cobalt / Q000737:chemistry; D003460:Crystallization; D045285:Desulfovibrio desulfuricans / Q000201:enzymology*; D004789:Enzyme Activation / Q000502:physiology; D004795:Enzyme Stability; D013430:Sulfate Adenylyltransferase / Q000737:chemistry* / Q000302:isolation & purification; D013431:Sulfates / Q000737:chemistry*; D014961:X-Ray Diffraction; D015032:Zinc / Q000737:chemistry
D001426:Bacterial Proteins; D013431:Sulfates; D003035:Cobalt; D013430:Sulfate Adenylyltransferase; D015032:Zinc