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Acta Crystallogr F Struct Biol Commun. 2016 Nov 1;72(Pt 11):831-839. Epub 2016 Oct 27.

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

Author information

1
School of Biosciences and Biotechnology, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, Bangi, Selangor Darul Ehsan 43600, Malaysia.
2
Infection and Immunity Program and the Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Monash University, Victoria 3800, Australia.
3
Department of Bioprocess Engineering, Faculty of Chemical Engineering, Universiti Teknologi Malaysia, 81310 Skudai, Johor Darul Takzim, Malaysia.
4
Malaysia Genome Institute, Jalan Bangi Lama, 43000 Kajang, Selangor Darul Ehsan, Malaysia.
5
Institute of Systems Biology (INBIOSIS), Universiti Kebangsaan Malaysia, 43600 Bangi, Selangor Darul Ehsan, Malaysia.

Abstract

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.

KEYWORDS:

Glaciozyma antarctica; crystallization; fuculose aldolase; imino cyclitols; l-fuculose metabolism; metalloenzymes; psychrophiles

PMID:
27827354
PMCID:
PMC5101584
DOI:
10.1107/S2053230X16015612
[Indexed for MEDLINE]
Free PMC Article

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