Preliminary characterization of two different crystal forms of acylphosphatase from the hyperthermophile archaeon Sulfolobus solfataricus

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Simone ZuccottiMartino Bolognesi

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 A resolution, respectively.

References

Mar 20, 1992·Journal of Molecular Biology·A PastoreR J Williams
Jan 15, 1997·Structure·M M ThunnissenP Nordlund
Feb 1, 1997·Cellular and Molecular Life Sciences : CMLS·M StefaniG Ramponi
May 26, 2004·Acta Crystallographica. Section D, Biological Crystallography·Simone ZuccottiMartino Bolognesi
Jun 24, 2004·Acta Crystallographica. Section D, Biological Crystallography·Yuk-Yin CheungKam-Bo Wong

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Citations

Mar 3, 2006·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Rachel C Y YeungKam-Bo Wong

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