› 4hwp

X-ray diffraction
1.81Å resolution

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

Released:
DOI: 10.2210/pdb4hwp/pdb
PDB entry 4hwp coloured by chain, front view.
PDB entry 4hwp coloured by chain, side view.
PDB entry 4hwp 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 X16 2 x X16
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 86.16Å b: 110.14Å c: 115.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.194 0.213
Expression system: Escherichia coli BL21

Quick links

Citations

7 review citations

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