PDBsum entry 2de0

Transferase

PDB id: 2de0

Contents

Protein chain

460 a.a. *

Waters ×137

* Residue conservation analysis

PDB id:

2de0

Name:

Transferase

Title:

Crystal structure of human alpha 1,6-fucosyltransferase, fut8

Structure:

Alpha-(1,6)-fucosyltransferase. Chain: x. Fragment: residues 68-575. Synonym: glycoprotein 6-alpha-l-fucosyltransferase, gdp-fucose-- glycoprotein fucosyltransferase, gdp-l-fuc:n-acetyl-beta-d- glucosaminide alpha1,6-fucosyltransferase, alpha1-6fuct, fucosyltransferase 8. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108.

Resolution:

2.61Å R-factor: 0.223 R-free: 0.283

Authors:

N.Taniguchi,H.Ihara,A.Nakagawa

Key ref:

H.Ihara et al. (2007). Crystal structure of mammalian alpha1,6-fucosyltransferase, FUT8. Glycobiology, 17, 455-466. PubMed id: 17172260

Date:

07-Feb-06 Release date: 26-Dec-06

Protein chain

Q9BYC5  (FUT8_HUMAN) -  Alpha-(1,6)-fucosyltransferase from Homo sapiens

Seq: 575 a.a.

Struc: 460 a.a.

Enzyme reactions

• Enzyme class: E.C.2.4.1.68 - glycoprotein 6-alpha-L-fucosyltransferase.
• Pathway: Mannosyl-glycoprotein ; fucosyl and xylosyl transferases
• Reaction: N₄-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)- alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D- GlcNAc}-L-asparaginyl-[protein] + GDP-beta-L-fucose = an N₄-{beta-D- GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man- (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-L-Fuc-(1->6)]-beta- D-GlcNAc}-L-asparaginyl-[protein] + GDP + H⁺

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

Glycobiology 17:455-466 (2007)

PubMed id: 17172260

Crystal structure of mammalian alpha1,6-fucosyltransferase, FUT8.

H.Ihara, Y.Ikeda, S.Toma, X.Wang, T.Suzuki, J.Gu, E.Miyoshi, T.Tsukihara, K.Honke, A.Matsumoto, A.Nakagawa, N.Taniguchi.

ABSTRACT

Mammalian alpha1,6-fucosyltransferase (FUT8) catalyses the transfer of a fucose residue from a donor substrate, guanosine 5'-diphosphate-beta-L-fucose to the reducing terminal N-acetylglucosamine (GlcNAc) of the core structure of an asparagine-linked oligosaccharide. Alpha1,6-fucosylation, also referred to as core fucosylation, plays an essential role in various pathophysiological events. Our group reported that FUT8 null mice showed severe growth retardation and emphysema-like lung-destruction as a result of the dysfunction of epidermal growth factor and transforming growth factor-beta receptors. To elucidate the molecular basis of FUT8 with respect to pathophysiology, the crystal structure of human FUT8 was determined at 2.6 A resolution. The overall structure of FUT8 was found to consist of three domains: an N-terminal coiled-coil domain, a catalytic domain, and a C-terminal SH3 domain. The catalytic region appears to be similar to GT-B glycosyltransferases rather than GT-A. The C-terminal part of the catalytic domain of FUT8 includes a Rossmann fold with three regions that are conserved in alpha1,6-, alpha1,2-, and protein O-fucosyltransferases. The SH3 domain of FUT8 is similar to other SH3 domain-containing proteins, although the significance of this domain remains to be elucidated. The present findings of FUT8 suggest that the conserved residues in the three conserved regions participate in the Rossmann fold and act as the donor binding site, or in catalysis, thus playing key roles in the fucose-transferring reaction.