Fucokinase/L-fucose-1-P-guanylyltransferase (FKP) is a bifunctional enzyme which converts L-fucose to Fuc-1-P and thence to GDP-L-fucose through the salvage pathway. The molecular weights of the full length FKP (F-FKP) and the C terminal truncated FKP (C-FKP, residues 300-949 amino acid) are 105.7 kDa and 71.7
kDa, respectively. In this study, both recombinant F-FKP and C-FKP were expressed and purified. Size exclusion experiments
showed both F-FKP and C-FKP have two different
oligomeric states and the lower oligomerics were predominant. Analytical ultracentrifugation results showed the lower oligomerics of F-FKP and C-FKP are trimers. F-FKP native protein was crystallized by vapour diffusion and its three dimensional feature was observed by Cryo-EM. The crystals belong to the space group P212121 and diffracted synchrotron X-rays to 3.7Å resolution. Crystal unit cell parameters are a=91.36Å, b=172.03Å, c=358.86Å, α=90.00º, β=90.00º, γ=90.00º, respectively. Considering the calculated Matthews coefficient of 2.19 with 43.83% solvent content, six molecules in one asymmetric unit is
proposed. The Cryo-EM image showed F-FKP
molecules is a-two-parallel disk-shaped objects stacking together, indicating two trimers are likely present in one asymmetric
unit. These preliminary crystallographic
and oligomeric analyse provide basic structure information of
FKP.