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

Jaafar, Nardiah Rizwana, Littler, Dene, Beddoe, Travis, Rossjohn, Jamie, Illias, Rosli Md, Mahadi, Nor Muhammad, Mackeen, Mukram Mohamed, Murad, Abdul Munir Abdul and Abu Bakar, Farah Diba 2016. Crystal structure of fuculose aldolase from the Antarctic psychrophilic yeastGlaciozyma antarctica PI12. Acta Crystallographica Section F Structural Biology Communications 72 (11) , pp. 831-839. 10.1107/S2053230X16015612

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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.

Item Type: Article
Date Type: Publication
Status: Published
Schools: Medicine
Publisher: International Union of Crystallography
ISSN: 2053-230X
Date of First Compliant Deposit: 10 July 2017
Date of Acceptance: 4 October 2016
Last Modified: 29 Jun 2019 15:05

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