› 1qkj

X-ray diffraction
2.3Å resolution

T4 Phage B-Glucosyltransferase, Substrate Binding and Proposed Catalytic Mechanism

Released:
DOI: 10.2210/pdb1qkj/pdb
PDB entry 1qkj coloured by chain, front view.
PDB entry 1qkj coloured by chain, side view.
PDB entry 1qkj coloured by chain, top view.
Source organism: Escherichia virus T4
Primary publication:
T4 phage beta-glucosyltransferase: substrate binding and proposed catalytic mechanism.
Moréra S, Imberty A, Aschke-Sonnenborn U, Rüger W, Freemont PS
J Mol Biol 292 717-30 (1999)
PMID: 10497034

Function and Biology Details

Reaction catalysed: 
Transfers a beta-D-glucosyl residue from UDP-alpha-D-glucose to a hydroxymethylcytosine residue in DNA
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domain:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137908 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA beta-glucosyltransferase Chain: A
Molecule details ›
Chain: A
Length: 351 amino acids
Theoretical weight: 40.72 KDa
Source organism: Escherichia virus T4
Expression system: Escherichia coli
UniProt:
  • Canonical: P04547 (Residues: 1-351; Coverage: 100%)
Gene name: bgt
Sequence domains: Bacteriophage T4 beta-glucosyltransferase
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM02
Spacegroup: P212121
Unit cell:
a: 69.46Å b: 102.47Å c: 59.42Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.19 0.29
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Structures and mechanisms of glycosyltransferases.
Breton et al. (2006)
10 more

2 mentions without citation

Bacteriophage T4 genome.
Miller et al. (2003)
1 more