› 1fyf

X-ray diffraction
1.65Å resolution

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

Released:
DOI: 10.2210/pdb1fyf/pdb
PDB entry 1fyf coloured by chain, front view.
PDB entry 1fyf coloured by chain, side view.
PDB entry 1fyf coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Transfer RNA-mediated editing in threonyl-tRNA synthetase. The class II solution to the double discrimination problem.
Dock-Bregeon A, Sankaranarayanan R, Romby P, Caillet J, Springer M, Rees B, Francklyn CS, Ehresmann C, Moras D
Cell 103 877-84 (2000)
PMID: 11136973

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
Molecule details ›
Chains: A, B
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 2 x ZN
Ligand SSA 2 x SSA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P212121
Unit cell:
a: 86.95Å b: 109.52Å c: 115.37Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.218 0.237
Expression system: Escherichia coli

Quick links

Citations

15 review citations

Structural insights into translational fidelity.
Ogle et al. (2005)
14 more

4 mentions without citation

Overview of protein structural and functional folds.
Sun et al. (2004)
3 more