Conserved structural features in eukaryotic and prokaryotic fucosyltransferases

Area of Science:

• Biochemistry
• Enzymology
• Molecular Biology

Background:

• Fucosyltransferases (FUTs) are crucial enzymes catalyzing the transfer of fucose from GDP-fucose to various acceptor molecules.
• Enzyme specificity is determined by acceptor recognition and the specific linkage formed (e.g., α1,2, α1,3, α1,4, α1,6).

Purpose of the Study:

• To investigate evolutionary relationships and conserved features among diverse fucosyltransferases.
• To classify fucosyltransferases based on sequence similarities and identify common structural and catalytic motifs.

Main Methods:

• Bioinformatic analysis of over 30 fucosyltransferase sequences from various organisms (mammals, chicken, nematode, bacteria).
• Protein sequence similarity searches and Hydrophobic Cluster Analysis (HCA) to identify conserved domains and motifs.

Main Results:

• Fucosyltransferases were initially classified into four families: α-2, α-3, mammalian α-6, and bacterial α-6 FUTs.
• HCA revealed a conserved peptide motif and structural features in α-2 and α-6 FUTs (prokaryotic and eukaryotic), grouping them into a superfamily.
• Strictly conserved amino acids, including two essential for human α-2 FUT activity, were identified within this superfamily.
• α-3 FUTs form a distinct family but share some similarities with α-2 and α-6 FUTs.

Conclusions:

• Fucosyltransferases exhibit significant evolutionary conservation, suggesting shared structural and catalytic properties.
• The identification of conserved motifs supports the classification of α-2 and α-6 FUTs into a single superfamily.
• Further research into conserved residues may elucidate fundamental mechanisms of fucosyltransferase activity.