Preliminary characterization of two different crystal forms of acylphosphatase from the hyperthermophile archaeon Sulfolobus solfataricus.
Acylphosphatase is a ubiquitous small enzyme that was first characterized in mammals. It is involved in the hydrolysis of carboxyl-phosphate bonds in several acylphosphate substrates, such as carbamoylphosphate and 1,3-biphosphoglycerate; however, a consensus on acylphosphatase action in vivo has not yet been reached. Recent investigations have focused on acylphosphatases from lower phyla, such as Drosophila melanogaster and Escherichia coli, in view of the application of these small proteins as models in the study of folding, misfolding and aggregation processes. An acylphosphatase from the hyperthermophilic archaeon Sulfolobus solfataricus has been cloned, expressed and purified. Here, the growth and characterization of a triclinic and a monoclinic crystal form of the hyperthermophilic enzyme are reported; X-ray diffraction data have been collected to 1.27 and 1.90 A resolution, respectively.
Zuccotti
Simone
S
Department of Physics-INFM, Center of Excellence for Biomedical Research, University of Genova, Via Dodecaneso 33, 16132 Genova, Italy.
Rosano
Camillo
C
Bemporad
Francesco
F
Stefani
Massimo
M
Bolognesi
Martino
M
D017766:Acid Anhydride Hydrolases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D003460:Crystallization; D008969:Molecular Sequence Data; D011489:Protein Denaturation; D017510:Protein Folding; D048229:Sulfolobus solfataricus / Q000201:enzymology*; D013816:Thermodynamics; D014961:X-Ray Diffraction; D000097024:Acylphosphatase
D017766:Acid Anhydride Hydrolases; D019843:Archaeal Proteins; D000097024:Acylphosphatase