› 1fr8

X-ray diffraction
2.4Å resolution

CRYSTAL STRUCTURE OF THE BOVINE BETA 1,4 GALACTOSYLTRANSFERASE (B4GALT1) CATALYTIC DOMAIN COMPLEXED WITH URIDINE DIPHOSPHOGALACTOSE

Released:
DOI: 10.2210/pdb1fr8/pdb
PDB entry 1fr8 coloured by chain, front view.
PDB entry 1fr8 coloured by chain, side view.
PDB entry 1fr8 coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Crystal structures of the bovine beta4galactosyltransferase catalytic domain and its complex with uridine diphosphogalactose.
Gastinel LN, Cambillau C, Bourne Y
EMBO J 18 3546-57 (1999)
PMID: 10393171

Function and Biology Details

Reactions catalysed: 
UDP-alpha-D-galactose + D-glucose = UDP + lactose
UDP-alpha-D-galactose + N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide = UDP + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
UDP-alpha-D-galactose + N-acetyl-beta-D-glucosaminylglycopeptide = UDP + beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminylglycopeptide
UDP-alpha-D-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139894 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Processed beta-1,4-galactosyltransferase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 288 amino acids
Theoretical weight: 33.07 KDa
Source organism: Bos taurus
Expression system: Mus musculus
UniProt:
  • Canonical: P08037 (Residues: 115-402; Coverage: 72%)
Gene names: B4GALT1, GALT, GGTB2
Sequence domains:
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

1 bound ligand:
Ligand GDU 2 x GDU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: C2221
Unit cell:
a: 104.72Å b: 161.37Å c: 106.31Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.237 0.262
Expression system: Mus musculus

Quick links

Citations

26 review citations

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

6 mentions without citation

Glycosyltransferase structural biology and its role in the design of catalysts for glycosylation.
Chang et al. (2011)
5 more