› 2jco

X-ray diffraction
2.57Å resolution

Crystal structure of wild type alpha-1,3 Galactosyltransferase in the absence of ligands

Released:
DOI: 10.2210/pdb2jco/pdb
PDB entry 2jco coloured by chain, front view.
PDB entry 2jco coloured by chain, side view.
PDB entry 2jco coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Conformational changes induced by binding UDP-2F-galactose to alpha-1,3 galactosyltransferase- implications for catalysis.
Jamaluddin H, Tumbale P, Withers SG, Acharya KR, Brew K
J Mol Biol 369 1270-81 (2007)
PMID: 17493636

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147073 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetyllactosaminide alpha-1,3-galactosyltransferase Chain: A
Molecule details ›
Chain: A
Length: 289 amino acids
Theoretical weight: 34.09 KDa
Source organism: Bos taurus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P14769 (Residues: 80-368; Coverage: 79%)
Gene name: GGTA1
Sequence domains: Glycosyltransferase family 6
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

1 bound ligand:
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: P41212
Unit cell:
a: 93.57Å b: 93.57Å c: 108.417Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.268 0.263 0.328
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

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

2 mentions without citation

Family 6 glycosyltransferases in vertebrates and bacteria: inactivation and horizontal gene transfer may enhance mutualism between vertebrates and bacteria.
Brew et al. (2010)
1 more