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PROSITE documentation PDOC51659

Glycosyltransferase family 23 (GT23) domain profile





Description

The fucosylation of glycoconjugates in mammalian organisms is related to a wide variety of biological preocesses, including cell adhesion, blood antigens, and some severe diseases including cancer metastasis, congenital disorders of glycosylation, and various microbial and virus infections. Fucosylation via α1,2-, α1,3- α1,4-, and α1,6-linkages, and protein O-fucosylation are accomplished by the cation of specific individual fucosyltransferases [1].

FUT8, a eukaryotic α1,6-fucosyltransferase, catalyzes the transfer of a fucosyl residue from guanine nucleotide diphosphate (GDP)-β-L-fucose to the reducing terminal N-acetylglucosamine (GlcNAc) of asparagine-linked oligosaccharides (N-glycan). The catalytic domain of FUT8 is structurally similar to that of NodZ, a bacterial α1,6-fucosyltransferase. NodZ plays a role in the synthesis of the Nod factor, which is involved in the nodulation of legume roots for nitrogen fixing, and is known to catalyze the α1,6-fucosylation of lipo-chitooligosaccharides and variations thereof, including chitooligosaccharides. Both the eukaryotic and bacterial fucoslytransferase are classified into the GT23 family of Carbohydrate-Active enZYmes [E1] and share GDP-β-L-fucose as the donor substrate. Although the acceptor substrates are different, a "common" chitobiose unit is contained in the reducing terminals of both substrates [2].

The GT23 domain is comprised of two structures, a N-terminal open sheet α/ β structure and a C-terminal Rossmann fold which is frequently found in nucleotide binding proteins including glycosyltransferases (see <PDB:2DE0>) [1,3,4].

The profile we developed covers the entire GT23 domain.

Last update:

October 2012 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

GT23, PS51659; Glycosyltransferase family 23 (GT23) domain profile  (MATRIX)


References

1AuthorsIhara H. Ikeda Y. Toma S. Wang X. Suzuki T. Gu J. Miyoshi E. Tsukihara T. Honke K. Matsumoto A. Nakagawa A. Taniguchi N.
TitleCrystal structure of mammalian alpha1,6-fucosyltransferase, FUT8.
SourceGlycobiology 17:455-466(2007).
PubMed ID17172260
DOI10.1093/glycob/cwl079

2AuthorsIhara H. Hanashima S. Okada T. Ito R. Yamaguchi Y. Taniguchi N. Ikeda Y.
TitleFucosylation of chitooligosaccharides by human alpha1,6-fucosyltransferase requires a nonreducing terminal chitotriose unit as a minimal structure.
SourceGlycobiology 20:1021-1033(2010).
PubMed ID20466647
DOI10.1093/glycob/cwq064

3AuthorsBrzezinski K. Stepkowski T. Panjikar S. Bujacz G. Jaskolski M.
TitleHigh-resolution structure of NodZ fucosyltransferase involved in the biosynthesis of the nodulation factor.
SourceActa Biochim. Pol. 54:537-549(2007).
PubMed ID17762900

4AuthorsBrzezinski K. Dauter Z. Jaskolski M.
TitleStructures of NodZ alpha1,6-fucosyltransferase in complex with GDP and GDP-fucose.
SourceActa Crystallogr. D 68:160-168(2012).
PubMed ID22281745
DOI10.1107/S0907444911053157

E1Sourcehttp://www.cazy.org/GT23.html



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