5KOP

Arabidopsis thaliana fucosyltransferase 1 (FUT1) in its apo-form

Summary for 5KOP

• Entry DOI: 10.2210/pdb5kop/pdb
• Descriptor: Galactoside 2-alpha-L-fucosyltransferase, CHLORIDE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: fucosyltransferase, apo-form, golgi, transferase
• Biological source: Arabidopsis thaliana (Thale cress)
• Total number of polymer chains: 4
• Total formula weight: 238048.40

Authors

Rocha, J.,de Sanctis, D.,Breton, C. (deposition date: 2016-07-01, release date: 2016-10-12, Last modification date: 2024-11-20)

Primary citation

Rocha, J.,Ciceron, F.,de Sanctis, D.,Lelimousin, M.,Chazalet, V.,Lerouxel, O.,Breton, C.
Structure of Arabidopsis thaliana FUT1 Reveals a Variant of the GT-B Class Fold and Provides Insight into Xyloglucan Fucosylation.
Plant Cell, 28:2352-2364, 2016

PubMed Abstract: The plant cell wall is a complex and dynamic network made mostly of cellulose, hemicelluloses, and pectins. Xyloglucan, the major hemicellulosic component in Arabidopsis thaliana, is biosynthesized in the Golgi apparatus by a series of glycan synthases and glycosyltransferases before export to the wall. A better understanding of the xyloglucan biosynthetic machinery will give clues toward engineering plants with improved wall properties or designing novel xyloglucan-based biomaterials. The xyloglucan-specific α2-fucosyltransferase FUT1 catalyzes the transfer of fucose from GDP-fucose to terminal galactosyl residues on xyloglucan side chains. Here, we present crystal structures of Arabidopsis FUT1 in its apoform and in a ternary complex with GDP and a xylo-oligosaccharide acceptor (named XLLG). Although FUT1 is clearly a member of the large GT-B fold family, like other fucosyltransferases of known structures, it contains a variant of the GT-B fold. In particular, it includes an extra C-terminal region that is part of the acceptor binding site. Our crystal structures support previous findings that FUT1 behaves as a functional dimer. Mutational studies and structure comparison with other fucosyltransferases suggest that FUT1 uses a S2-like reaction mechanism similar to that of protein-O-fucosyltransferase 2. Thus, our results provide new insights into the mechanism of xyloglucan fucosylation in the Golgi.

PubMed: 27637560
DOI: 10.1105/tpc.16.00519

Experimental method

X-RAY DIFFRACTION (2.1 Å)