› 2cya

X-ray diffraction
2.2Å resolution

Crystal structure of tyrosyl-tRNA synthetase from Aeropyrum pernix

Released:
DOI: 10.2210/pdb2cya/pdb
PDB entry 2cya coloured by chain, front view.
PDB entry 2cya coloured by chain, side view.
PDB entry 2cya coloured by chain, top view.
Source organism: Aeropyrum pernix
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-195437 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine--tRNA ligase Chain: A
Molecule details ›
Chain: A
Length: 364 amino acids
Theoretical weight: 40.83 KDa
Source organism: Aeropyrum pernix
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9YA64 (Residues: 1-364; Coverage: 100%)
Gene names: APE_2074.1, tyrS
Sequence domains: tRNA synthetases class I (W and Y)
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P43212
Unit cell:
a: 65.912Å b: 65.912Å c: 196.168Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.211 0.238
Expression system: Escherichia coli

Quick links

Citations

5 review citations

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

1 mention without citation

The double-length tyrosyl-tRNA synthetase from the eukaryote Leishmania major forms an intrinsically asymmetric pseudo-dimer.
Larson et al. (2011)