4XXF

L-fuculose 1-phosphate aldolase from Glaciozyma antarctica PI12

Summary for 4XXF

• Entry DOI: 10.2210/pdb4xxf/pdb
• Descriptor: Fuculose-1-phosphate aldolase, ZINC ION (3 entities in total)
• Functional Keywords: fuculose 1-phosphate aldolase, psychrophiles, metalloenzyme, lyase
• Biological source: Glaciozyma antarctica
• Total number of polymer chains: 1
• Total formula weight: 28236.55

Authors

Jaafar, N.R.,Abu Bakar, F.D.,Abdul Murad, A.M.,Illias, R.,Littler, D.,Beddoe, T.,Rossjohn, J.,Mahadi, M.N. (deposition date: 2015-01-30, release date: 2015-02-25, Last modification date: 2023-11-08)

Primary citation

Jaafar, N.R.,Littler, D.,Beddoe, T.,Rossjohn, J.,Illias, R.M.,Mahadi, N.M.,Mackeen, M.M.,Murad, A.M.,Abu Bakar, F.D.
Crystal structure of fuculose aldolase from the Antarctic psychrophilic yeast Glaciozyma antarctica PI12.
Acta Crystallogr.,Sect.F, 72:831-839, 2016

PubMed 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.

PubMed: 27827354
DOI: 10.1107/S2053230X16015612

Experimental method

X-RAY DIFFRACTION (1.34 Å)