› 1evl

X-ray diffraction
1.55Å resolution

CRYSTAL STRUCTURE OF A TRUNCATED FORM OF THREONYL-TRNA SYNTHETASE WITH A THREONYL ADENYLATE ANALOG

Released:
DOI: 10.2210/pdb1evl/pdb
PDB entry 1evl coloured by chain, front view.
PDB entry 1evl coloured by chain, side view.
PDB entry 1evl coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Zinc ion mediated amino acid discrimination by threonyl-tRNA synthetase.
Sankaranarayanan R, Dock-Bregeon AC, Rees B, Bovee M, Caillet J, Romby P, Francklyn CS, Moras D
Nat Struct Biol 7 461-5 (2000)
PMID: 10881191

Function and Biology Details

Reaction catalysed: 
ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141713 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Threonine--tRNA ligase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 401 amino acids
Theoretical weight: 46.73 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A8M3 (Residues: 242-642; Coverage: 63%)
Gene names: JW1709, b1719, thrS
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 4 x ZN
Ligand TSB 4 x TSB
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P21
Unit cell:
a: 86.7Å b: 111.1Å c: 135.2Å
α: 90° β: 93.5° γ: 90°
R-values:
R R work R free
0.22 0.215 0.226
Expression system: Escherichia coli

Quick links

Citations

13 review citations

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

9 mentions without citation

In silico discovery of aminoacyl-tRNA synthetase inhibitors.
Zhao et al. (2014)
8 more