› 2vs5

X-ray diffraction
1.82Å resolution

THE BINDING OF UDP-GALACTOSE BY AN ACTIVE SITE MUTANT OF alpha-1,3 GALACTOSYLTRANSFERASE (alpha3GT)

Released:
DOI: 10.2210/pdb2vs5/pdb
PDB entry 2vs5 coloured by chain, front view.
PDB entry 2vs5 coloured by chain, side view.
PDB entry 2vs5 coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Structural basis of UDP-galactose binding by alpha-1,3-galactosyltransferase (alpha3GT): role of negative charge on aspartic acid 316 in structure and activity.
Tumbale P, Jamaluddin H, Thiyagarajan N, Brew K, Acharya KR
Biochemistry 47 8711-8 (2008)
PMID: 18651752

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 286 amino acids
Theoretical weight: 33.76 KDa
Source organism: Bos taurus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P14769 (Residues: 80-365; Coverage: 78%)
Gene name: GGTA1
Sequence domains: Glycosyltransferase family 6
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

3 bound ligands:
Ligand MN 3 x MN
Ligand GDU 2 x GDU
Ligand MPD 1 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.2
Spacegroup: P212121
Unit cell:
a: 87.027Å b: 91.37Å c: 94.63Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.236 0.242
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

A molecular description of cellulose biosynthesis.
McNamara et al. (2015)
9 other articles

3 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)
2 more