1sxq

X-ray diffraction
1.8Å resolution

BGT in complex with a 13mer DNA containing a central C:G base pair and UDP

Released:
Source organism: Escherichia virus T4
Primary publication:
Structural evidence of a passive base-flipping mechanism for beta-glucosyltransferase.
J. Biol. Chem. 279 34715-20 (2004)
PMID: 15178685

Function and Biology Details

Reaction catalysed:
Transfers a beta-D-glucosyl residue from UDP-alpha-D-glucose to a hydroxymethylcytosine residue in DNA
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
Macromolecules (3 distinct):
DNA beta-glucosyltransferase Chains: A, B
Molecule details ›
Chains: A, B
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;
5'-D(*AP*AP*AP*AP*AP*AP*GP*TP*TP*TP*TP*TP*T)-3' Chains: C, D
Molecule details ›
Chains: C, D
Length: 13 nucleotides
Theoretical weight: 3.99 KDa
Source organism: Escherichia virus T4
Expression system: Not provided
5'-D(*AP*AP*AP*AP*AP*AP*CP*TP*TP*TP*TP*TP*T)-3' Chains: E, F
Molecule details ›
Chains: E, F
Length: 13 nucleotides
Theoretical weight: 3.95 KDa
Source organism: Escherichia virus T4
Expression system: Not provided

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 72.652Å b: 70.157Å c: 96.581Å
α: 90° β: 90.55° γ: 90°
R-values:
R R work R free
0.183 0.183 0.212
Expression systems:
  • Escherichia coli
  • Not provided