Crystal structure of fuculose aldolase from the Antarctic psychrophilic yeastGlaciozyma antarctica PI12

• Published in: Acta Crystallographica Section F Structural Biology Communications
• Main Authors: 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
• Format: Article in Journal/Newspaper
• Language: English
• Published: International Union of Crystallography 2016
• Subjects: Antarctic; The Antarctic; Antarc*; Antarctica
• Online Access: https://orca.cardiff.ac.uk/id/eprint/102231/; https://doi.org/10.1107/S2053230X16015612; https://orca.cardiff.ac.uk/id/eprint/102231/1/Crystal%20structure%20fuculose%20Rossjohn-Jaafar.pdf

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.