7YRO

Crystal structure of mango fucosyltransferase 13

Summary for 7YRO

• Entry DOI: 10.2210/pdb7yro/pdb
• Descriptor: Fucosyltransferase, GLYCEROL, ACETIC ACID, ... (7 entities in total)
• Functional Keywords: fucosyltransferase, fut13, mango, transferase
• Biological source: Mangifera indica (mango)
• Total number of polymer chains: 8
• Total formula weight: 374090.49

Authors

Okada, T.,Teramoto, T.,Ihara, H.,Ikeda, Y.,Kakuta, Y. (deposition date: 2022-08-10, release date: 2023-08-16, Last modification date: 2026-03-04)

Primary citation

Okada, T.,Teramoto, T.,Ihara, H.,Ikeda, Y.,Kakuta, Y.
Crystal structure of mango alpha 1,3/ alpha 1,4-fucosyltransferase elucidates unique elements that regulate Lewis A-dominant oligosaccharide assembly.
Glycobiology, 34:-, 2024

PubMed Abstract: In various organisms, α1,3/α1,4-fucosyltransferases (CAZy GT10 family enzymes) mediate the assembly of type I (Galβ1,3GlcNAc) and/or type II (Galβ1,4GlcNAc)-based Lewis structures that are widely distributed in glycoconjugates. Unlike enzymes of other species, plant orthologues show little fucosyltransferase activity for type II-based glycans and predominantly catalyze the assembly of the Lewis A structure [Galβ1,3(Fucα1,4)GlcNAc] on the type I disaccharide unit of their substrates. However, the structural basis underlying this unique substrate selectivity remains elusive. In this study, we investigated the structure-function relationship of MiFUT13A, a mango α1,3/α1,4-fucosyltransferase. The prepared MiFUT13A displayed distinct α1,4-fucosyltransferase activity. Consistent with the enzymatic properties of this molecule, X-ray crystallography revealed that this enzyme has a typical GT-B fold-type structure containing a set of residues that are responsible for its SN2-like catalysis. Site-directed mutagenesis and molecular docking analyses proposed a rational binding mechanism for type I oligosaccharides. Within the catalytic cleft, the pocket surrounding Trp121 serves as a binding site, anchoring the non-reducing terminal β1,3-galactose that belongs to the type I disaccharide unit. Furthermore, Glu177 was postulated to function as a general base catalyst through its interaction with the 4-hydroxy group of the acceptor N-acetylglucosamine residue. Adjacent residues, specifically Thr120, Thr157 and Asp175 were speculated to assist in binding of the reducing terminal residues. Intriguingly, these structural elements were not fully conserved in mammalian orthologue which also shows predominant α1,4-fucosyltransferase activity. In conclusion, we have proposed that MiFUT13A generates the Lewis A structure on type I glycans through a distinct mechanism, divergent from that of mammalian enzymes.

PubMed: 38376259
DOI: 10.1093/glycob/cwae015

Experimental method

X-RAY DIFFRACTION (2.42 Å)