› 2vce

X-ray diffraction
1.9Å resolution

Characterization and engineering of the bifunctional N- and O- glucosyltransferase involved in xenobiotic metabolism in plants

Released:
DOI: 10.2210/pdb2vce/pdb
PDB entry 2vce coloured by chain, front view.
PDB entry 2vce coloured by chain, side view.
PDB entry 2vce coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Characterization and engineering of the bifunctional N- and O-glucosyltransferase involved in xenobiotic metabolism in plants.
Brazier-Hicks M, Offen WA, Gershater MC, Revett TJ, Lim EK, Bowles DJ, Davies GJ, Edwards R
Proc Natl Acad Sci U S A 104 20238-43 (2007)
PMID: 18077347

Function and Biology Details

Reaction catalysed: 
UDP-glucose + hydroquinone = UDP + hydroquinone-O-beta-D-glucopyranoside
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192356 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-glycosyltransferase 72B1 Chain: A
Molecule details ›
Chain: A
Length: 480 amino acids
Theoretical weight: 52.99 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9M156 (Residues: 1-480; Coverage: 100%)
Gene names: At4g01070, F2N1.15, UGT72B1
Sequence domains: UDP-glucoronosyl and UDP-glucosyl transferase
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments

3 bound ligands:
Ligand U2F 1 x U2F
Ligand TC7 1 x TC7
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 47.807Å b: 94.335Å c: 57.059Å
α: 90° β: 110.31° γ: 90°
R-values:
R R work R free
0.16 0.158 0.198
Expression system: Escherichia coli

Quick links

Citations

22 review citations

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

25 mentions without citation

Glycosyltransferase structural biology and its role in the design of catalysts for glycosylation.
Chang et al. (2011)
24 more