2.4.1.68: glycoprotein 6-alpha-L-fucosyltransferase
This is an abbreviated version!
For detailed information about glycoprotein 6-alpha-L-fucosyltransferase, go to the full flat file.
Word Map on EC 2.4.1.68
Reaction
Synonyms
6FucT, alfC, alpha(1,6)FT, alpha(1,6)fucosyltransferase, alpha-1,6-fucosyltransferase, alpha-6-fucosyltransferase, alpha1,6-fucosyltransferase, alpha1,6-FucT, alpha1,6FucT, alpha1-6,fucosyltransferase, alpha1-6FucT, alpha6FucT, BN194_28780, fucosyltransferase 8, fucosyltransferase, guanosine diphosphofucose-glycoprotein, FUT8, GDP-fucose glycoprotein fucosyltransferase, GDP-fucose-glycoprotein fucosyltransferase, GDP-L-fuc:N-acetyl-beta-D-glucosaminide alpha1-6fucosyltransferase, GDP-L-fucose-glycoprotein fucosyltransferase, GDP-L-fucose:2-acetamido-2-deoxy-beta-D-glucoside 6-alpha-L-fucosyltransferase, GDPfucose glycoprotein fucosyltransferase, glycoprotein fucosyltransferase, guanosine diphosphofucose-glycoprotein fucosyltransferase, NodZ, NodZ fucosyltransferase
ECTree
2.4.1.68 glycoprotein 6-alpha-L-fucosyltransferaseAdvanced search results
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results (Crystallization
Crystallization on EC 2.4.1.68 - glycoprotein 6-alpha-L-fucosyltransferase
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CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
in complex with GDP and GDP-fucose, using 350 mM potassium sodium tartrate, 100 mM MES pH 6.5 and 50 mM MgCl2
NodZ protein is crystallized in the presence of phosphate ions in two crystal forms. The enzyme is arranged into two domains of nearly equal size. Although NodZ falls in one broad class (GT-B) with other two-domain glycosyltransferases, the topology of its domains deviates from the canonical Rossmann fold, with particularly high distortions in the N-terminal domain
hanging drop vapor diffusion method, crystal structure at 2.6 A resolution
molecular modeling predicts homophilic dimerization. Residues Ala123, Leu130, and Leu137 of alpha1-helix, and Ala149, Leu156, Ile163, Leu170 of the alpha2-helix all contribute to the formation of the hydrophobic core in the four alpha-helices bundle. The bundle is formed via intermolecular and intramolecular hydrophobic interactions and provides an interface for other intermolecular interactions. In the prediction, each of the SH3 domains is located in close proximity to the interface formed by the alpha-helical domain of the counterpart in the predicted dimer
structure of FUT8 complexed with GDP and a biantennary complex N-glycan (G0). FUT8 follows an SN2 mechanism and deploys a series of loops and an alpha-helix which all contribute in forming the binding site. An exosite, formed by one of these loops and an SH3 domain, is responsible for the recognition of branched sugars, making contacts specifically to the alpha-1,3 arm GlcNAc, required for catalysis
