› 1tke

X-ray diffraction
1.46Å resolution

Crystal structure of the editing domain of threonyl-tRNA synthetase complexed with serine

Released:
DOI: 10.2210/pdb1tke/pdb
PDB entry 1tke coloured by chain, front view.
PDB entry 1tke coloured by chain, side view.
PDB entry 1tke coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Achieving error-free translation; the mechanism of proofreading of threonyl-tRNA synthetase at atomic resolution.
Dock-Bregeon AC, Rees B, Torres-Larios A, Bey G, Caillet J, Moras D
Mol Cell 16 375-86 (2004)
PMID: 15525511

Function and Biology Details

Reaction catalysed: 
ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141711 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Threonine--tRNA ligase Chain: A
Molecule details ›
Chain: A
Length: 224 amino acids
Theoretical weight: 25.47 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0A8M3 (Residues: 1-224; Coverage: 35%)
Gene names: JW1709, b1719, thrS
Sequence domains:
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 43.697Å b: 44.913Å c: 116.607Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.178 0.207
Expression system: Escherichia coli BL21

Quick links

Citations

10 review citations

Aminoacyl-tRNA synthesis and translational quality control.
Ling et al. (2009)
9 more

1 mention without citation

Calculating ensemble averaged descriptions of protein rigidity without sampling.
González et al. (2012)