Crystal structure of fuculose aldolase from the Antarctic psychrophilic yeast Glaciozyma antarctica PI12

In this study, the gene encoding FucA from Glaciozyma antarctica PI12 (GaFucA) was cloned and the enzyme was overexpressed in Escherichia coli, purified and crystallized. The tetrameric structure of GaFucA was determined to 1.34   Å resolution. The overall architecture of GaFucA and its catalytically essential histidine triad are highly conserved among other fuculose aldolases. Comparisons of structural features between GaFucA and its mesophilic and thermophilic homologues revealed that the enzyme has typical psychrophilic attributes, indicated by the presence of a high number of nonpolar residues at the surface and a lower number of arginine residues.

Source: Acta Crystallographica Section F - October 26, 2016 Category: Biochemistry Authors: Jaafar, N.R. Littler, D. Beddoe, T. Rossjohn, J. Illias, R.M. Mahadi, N.M. Mackeen, M.M. Murad, A.M.A. Abu Bakar, F.D. Tags: psychrophiles crystallization metalloenzymes fuculose aldolase l-fuculose metabolism Glaciozyma antarctica imino cyclitols research communications Source Type: research