› 4hwr

X-ray diffraction
1.9Å resolution

Crystal structure of E. coli Threonyl-tRNA synthetase bound to a novel inhibitor

Released:
DOI: 10.2210/pdb4hwr/pdb
PDB entry 4hwr coloured by chain, front view.
PDB entry 4hwr coloured by chain, side view.
PDB entry 4hwr coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Identification of bacteria-selective threonyl-tRNA synthetase substrate inhibitors by structure-based design.
Teng M, Hilgers MT, Cunningham ML, Borchardt A, Locke JB, Abraham S, Haley G, Kwan BP, Hall C, Hough GW, Shaw KJ, Finn J
J Med Chem 56 1748-60 (2013)
PMID: 23362938

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 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
Molecule details ›
Chains: A, B
Length: 411 amino acids
Theoretical weight: 48 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21
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 2 x ZN
Ligand 1B2 2 x 1B2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: C2
Unit cell:
a: 156.899Å b: 109.777Å c: 86.995Å
α: 90° β: 123.76° γ: 90°
R-values:
R R work R free
0.267 0.266 0.303
Expression system: Escherichia coli BL21

Quick links

Citations

5 review citations

Progress and challenges in aminoacyl-tRNA synthetase-based therapeutics.
Francklyn et al. (2019)
4 more

2 mentions without citation

Aminoacyl-tRNA Synthetases as Valuable Targets for Antimicrobial Drug Discovery.
Pang et al. (2021)
1 more