Premium
Crystal structure of fuculose aldolase from the Antarctic psychrophilic yeast Glaciozyma antarctica PI12
Author(s) -
Jaafar Nardiah Rizwana,
Littler Dene,
Beddoe Travis,
Rossjohn Jamie,
Illias Rosli Md,
Mahadi Nor Muhammad,
Mackeen Mukram Mohamed,
Murad Abdul Munir Abdul,
Abu Bakar Farah Diba
Publication year - 2016
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x16015612
Subject(s) - psychrophile , yeast , aldolase a , chemistry , crystallography , biochemistry , astrobiology , biology , enzyme
Fuculose‐1‐phosphate aldolase (FucA) catalyses the reversible cleavage of l ‐fuculose 1‐phosphate to dihydroxyacetone phosphate (DHAP) and l ‐lactaldehyde. This enzyme from mesophiles and thermophiles has been extensively studied; however, there is no report on this enzyme from a psychrophile. 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.