› 4ee3

X-ray diffraction
2.3Å resolution

Crystal structure of human M340H-beta-1,4-galactosyltransferase-1 (M340H-B4GAL-T1) in complex with pentasaccharide

Released:
DOI: 10.2210/pdb4ee3/pdb
PDB entry 4ee3 coloured by chain, front view.
PDB entry 4ee3 coloured by chain, side view.
PDB entry 4ee3 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Binding of N-acetylglucosamine (GlcNAc) β1-6-branched oligosaccharide acceptors to β4-galactosyltransferase I reveals a new ligand binding mode.
Ramakrishnan B, Boeggeman E, Qasba PK
J Biol Chem 287 28666-74 (2012)
PMID: 22740701

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 analysis Details

Assemblies composition:
monomeric (preferred)
homo hexamer
homo trimer
Assembly name:
PDBe Complex ID:
PDB-CPX-147296 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Beta-1,4-galactosyltransferase 1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 287 amino acids
Theoretical weight: 32.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P15291 (Residues: 126-398; Coverage: 69%)
Gene names: B4GALT1, GGTB2
Sequence domains:
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC, GAL, NAG
Carbohydrate polymer
4 bound ligands:
Ligand UDH 3 x UDH
Ligand MN 3 x MN
Ligand SO4 18 x SO4
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2221
Unit cell:
a: 107.612Å b: 195.158Å c: 143.695Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.187 0.24
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

Enzymatic glycosylation of multivalent scaffolds.
Bojarová et al. (2013)
1 more

4 mentions without citation

Conformations of the type-1 lacto-N-biose I unit in protein complex structures.
Fushinobu S. (2018)
3 more