TY - JOUR
T1 - Crystal structure of fuculose aldolase from the Antarctic psychrophilic yeast Glaciozyma antarctica PI12
AU - Jaafar, Nardiah Rizwana
AU - Littler, Dene
AU - Beddoe, Travis
AU - Rossjohn, Jamie
AU - Illias, Rosli Md
AU - Mahadi, Nor Muhammad
AU - Mackeen, Mukram Mohamed
AU - Murad, Abdul Munir Abdul
AU - Bakar, Farah Diba Abu
PY - 2016/11
Y1 - 2016/11
N2 - 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.
AB - 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.
KW - crystallization
KW - fuculose aldolase
KW - Glaciozyma antarctica
KW - imino cyclitols
KW - l-fuculose metabolism
KW - metalloenzymes
KW - psychrophiles
UR - https://www.scopus.com/pages/publications/84994777541
U2 - 10.1107/S2053230X16015612
DO - 10.1107/S2053230X16015612
M3 - Article
AN - SCOPUS:84994777541
SN - 1744-3091
VL - F72
SP - 831
EP - 839
JO - Acta Crystallographica Section F: Structural Biology Communications
JF - Acta Crystallographica Section F: Structural Biology Communications
IS - 11
ER -