› 1h3f

X-ray diffraction
2Å resolution

Tyrosyl-tRNA synthetase from Thermus thermophilus complexed with tyrosinol

Released:
DOI: 10.2210/pdb1h3f/pdb
PDB entry 1h3f coloured by chain, front view.
PDB entry 1h3f coloured by chain, side view.
PDB entry 1h3f coloured by chain, top view.
Source organism: Thermus thermophilus HB27
Primary publication:
Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition.
Yaremchuk A, Kriklivyi I, Tukalo M, Cusack S
EMBO J 21 3829-40 (2002)
PMID: 12110594

Function and Biology Details

Reaction catalysed: 
ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr)
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-160695 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine--tRNA ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 432 amino acids
Theoretical weight: 48.79 KDa
Source organism: Thermus thermophilus HB27
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P83453 (Residues: 1-432; Coverage: 100%)
Gene names: TT_C1033, tyrS
Sequence domains: tRNA synthetases class I (W and Y)
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 5 x SO4
Ligand TYE 2 x TYE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 67.794Å b: 111.05Å c: 141.226Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.234 0.234 0.261
Expression system: Escherichia coli BL21(DE3)

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Citations

14 review citations

Aminoacyl-tRNA synthetases: versatile players in the changing theater of translation.
Francklyn et al. (2002)
13 more

6 mentions without citation

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