› 1uqt

X-ray diffraction
2Å resolution

Trehalose-6-phosphate from E. coli bound with UDP-2-fluoro glucose.

Released:
DOI: 10.2210/pdb1uqt/pdb
PDB entry 1uqt coloured by chain, front view.
PDB entry 1uqt coloured by chain, side view.
PDB entry 1uqt coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The donor subsite of trehalose-6-phosphate synthase: binary complexes with UDP-glucose and UDP-2-deoxy-2-fluoro-glucose at 2 A resolution.
Gibson RP, Tarling CA, Roberts S, Withers SG, Davies GJ
J Biol Chem 279 1950-5 (2004)
PMID: 14570926

Function and Biology Details

Reaction catalysed: 
UDP-alpha-D-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152067 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trehalose-6-phosphate synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 482 amino acids
Theoretical weight: 54.75 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P31677 (Residues: 1-474; Coverage: 100%)
Gene names: JW5312, b1896, otsA
Sequence domains: Glycosyltransferase family 20
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments

1 bound ligand:
Ligand U2F 2 x U2F
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF
Spacegroup: P21212
Unit cell:
a: 88.919Å b: 101.521Å c: 118.207Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.219 0.251
Expression system: Escherichia coli BL21(DE3)

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Citations

7 review citations

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

6 mentions without citation

O-GlcNAc transferase invokes nucleotide sugar pyrophosphate participation in catalysis.
Schimpl et al. (2012)
5 more