› 1x8x

X-ray diffraction
2Å resolution

Tyrosyl t-RNA Synthetase from E.coli Complexed with Tyrosine

Released:
DOI: 10.2210/pdb1x8x/pdb
PDB entry 1x8x coloured by chain, front view.
PDB entry 1x8x coloured by chain, side view.
PDB entry 1x8x coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural snapshots of the KMSKS loop rearrangement for amino acid activation by bacterial tyrosyl-tRNA synthetase.
Kobayashi T, Takimura T, Sekine R, Kelly VP, Vincent K, Kamata K, Sakamoto K, Nishimura S, Yokoyama S
J Mol Biol 346 105-17 (2005)
PMID: 15663931

Function and Biology Details

Reaction catalysed: 
ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142837 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine--tRNA ligase Chain: A
Molecule details ›
Chain: A
Length: 322 amino acids
Theoretical weight: 36.07 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AGJ9 (Residues: 1-322; Coverage: 76%)
Gene names: JW1629, b1637, tyrS
Sequence domains: tRNA synthetases class I (W and Y)
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 1 x SO4
Ligand TYR 1 x TYR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL32B2
Spacegroup: P3121
Unit cell:
a: 82.82Å b: 82.82Å c: 93.49Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.191 0.22
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Expanding the genetic code.
Wang et al. (2006)
3 more

18 mentions without citation

Non-canonical Amino Acid Substrates of E. coli Aminoacyl-tRNA Synthetases.
Hartman MCT. (2022)
17 more