› 2cyc

X-ray diffraction
2.2Å resolution

Crystal structure of Tyrosyl-tRNA Synthetase complexed with L-tyrosine from Pyrococcus horikoshii

Released:
DOI: 10.2210/pdb2cyc/pdb
PDB entry 2cyc coloured by chain, front view.
PDB entry 2cyc coloured by chain, side view.
PDB entry 2cyc coloured by chain, top view.
Source organism: Pyrococcus horikoshii OT3
Primary publication:
Crystal structures of tyrosyl-tRNA synthetases from Archaea.
Kuratani M, Sakai H, Takahashi M, Yanagisawa T, Kobayashi T, Murayama K, Chen L, Liu ZJ, Wang BC, Kuroishi C, Kuramitsu S, Terada T, Bessho Y, Shirouzu M, Sekine S, Yokoyama S
J Mol Biol 355 395-408 (2006)
PMID: 16325203

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 analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129763 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine--tRNA ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 375 amino acids
Theoretical weight: 43.34 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
UniProt:
  • Canonical: O58739 (Residues: 1-375; Coverage: 100%)
Gene names: PH1011, tyrS
Sequence domains: tRNA synthetases class I (W and Y)
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand TYR 2 x TYR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: P212121
Unit cell:
a: 74.35Å b: 88.26Å c: 162.92Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.171 0.217
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Adenylate-forming enzymes.
Schmelz et al. (2009)
4 more

3 mentions without citation

Predicted class-I aminoacyl tRNA synthetase-like proteins in non-ribosomal peptide synthesis.
Aravind et al. (2010)
2 more