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

Nardiah Rizwana Jaafar; Dene Littler; Travis Beddoe; Jamie Rossjohn; Rosli Md Illias; Nor Muhammad Mahadi; Mukram Mohamed Mackeen; Abdul Munir Abdul Murad; Farah Diba Abu Bakar

doi:10.1107/S2053230X16015612

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

Acta Crystallogr F Struct Biol Commun. 2016 Nov 1;72(Pt 11):831-839. doi: 10.1107/S2053230X16015612. Epub 2016 Oct 27.

Authors

Nardiah Rizwana Jaafar¹, Dene Littler², Travis Beddoe², Jamie Rossjohn², Rosli Md Illias³, Nor Muhammad Mahadi⁴, Mukram Mohamed Mackeen⁵, Abdul Munir Abdul Murad¹, Farah Diba Abu Bakar¹

Affiliations

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.

MeSH terms

Aldehyde-Lyases / chemistry*
Aldehyde-Lyases / genetics
Aldehyde-Lyases / metabolism
Amino Acid Sequence
Antarctic Regions
Binding Sites
Catalytic Domain
Cloning, Molecular
Crystallography, X-Ray
Dihydroxyacetone Phosphate / chemistry*
Dihydroxyacetone Phosphate / metabolism
Enzyme Stability
Escherichia coli / genetics
Escherichia coli / metabolism
Fungal Proteins / chemistry*
Fungal Proteins / genetics
Fungal Proteins / metabolism
Gene Expression
Hexosephosphates / chemistry*
Hexosephosphates / metabolism
Models, Molecular
Plasmids / chemistry
Plasmids / metabolism
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Protein Multimerization
Recombinant Proteins / chemistry
Recombinant Proteins / genetics
Recombinant Proteins / metabolism
Saccharomycetales / chemistry*
Saccharomycetales / enzymology
Sequence Alignment
Sequence Homology, Amino Acid

Substances

Fungal Proteins
Hexosephosphates
Recombinant Proteins
fuculose 1-phosphate
Dihydroxyacetone Phosphate
Aldehyde-Lyases
L-fuculosephosphate aldolase