Preliminary characterization of two different crystal forms of acylphosphatase from the hyperthermophile archaeon Sulfolobus solfataricus
Articolo
Data di Pubblicazione:
2005
Citazione:
Preliminary characterization of two different crystal forms of acylphosphatase from the hyperthermophile archaeon Sulfolobus solfataricus / S. Zuccotti, C. Rosano, F. Bemporad, M. Stefani, M. Bolognesi. - In: ACTA CRYSTALLOGRAPHICA. SECTION F, STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS. - ISSN 1744-3091. - 61:1(2005 Jan), pp. 144-146.
Abstract:
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 Å resolution, respectively.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
acylphosphatase ; hyperthermophilic protein ; Sulfolobus solfataricus ; archaea proteins ; protein crystals
Elenco autori:
S. Zuccotti, C. Rosano, F. Bemporad, M. Stefani, M. Bolognesi
Link alla scheda completa: