› 2nzx

X-ray diffraction
1.9Å resolution

Crystal Structure of alpha1,3-Fucosyltransferase with GDP

Released:
DOI: 10.2210/pdb2nzx/pdb
PDB entry 2nzx coloured by chain, front view.
PDB entry 2nzx coloured by chain, side view.
PDB entry 2nzx coloured by chain, top view.
Source organism: Helicobacter pylori
Primary publication:
Structure and mechanism of Helicobacter pylori fucosyltransferase. A basis for lipopolysaccharide variation and inhibitor design.
Sun HY, Lin SW, Ko TP, Pan JF, Liu CL, Lin CN, Wang AH, Lin CH
J Biol Chem 282 9973-9982 (2007)
PMID: 17251184

Function and Biology Details

Reaction catalysed: 
GDP-beta-L-fucose + beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl-R = GDP + beta-D-galactosyl-(1->4)-(alpha-L-fucosyl-(1->3))-N-acetyl-D-glucosaminyl-R
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128249 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-(1,3)-fucosyltransferase FucT Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 371 amino acids
Theoretical weight: 43.12 KDa
Source organism: Helicobacter pylori
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O30511 (Residues: 1-363; Coverage: 76%)
Gene name: fucT
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand GDP 3 x GDP
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL12B2
Spacegroup: P21212
Unit cell:
a: 104.154Å b: 136.249Å c: 96.375Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.19 0.237
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

Glycosyltransferases: structures, functions, and mechanisms.
Lairson et al. (2008)
12 more

1 mention without citation

Effects of the difference in similarity measures on the comparison of ligand-binding pockets using a reduced vector representation of pockets.
Nakamura et al. (2016)