› 1v4p

X-ray diffraction
1.45Å resolution

Crystal structure of Alanyl-tRNA Synthetase from Pyrococcus horikoshii OT3

Released:
DOI: 10.2210/pdb1v4p/pdb
PDB entry 1v4p coloured by chain, front view.
PDB entry 1v4p coloured by chain, side view.
PDB entry 1v4p coloured by chain, top view.
Source organism: Pyrococcus horikoshii
Primary publication:
Crystal structure of alanyl-tRNA synthetase editing-domain homolog (PH0574) from a hyperthermophile, Pyrococcus horikoshii OT3 at 1.45 A resolution.
Ishijima J, Uchida Y, Kuroishi C, Tuzuki C, Takahashi N, Okazaki N, Yutani K, Miyano M
Proteins 62 1133-7 (2006)
PMID: 16374837

Function and Biology Details

Reaction catalysed: 
ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Biochemical function:
Biological process:
Cellular component:
Sequence domain:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-129701 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alanyl-tRNA editing protein AlaX-S Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 157 amino acids
Theoretical weight: 18.18 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli
UniProt:
  • Canonical: O58307 (Residues: 1-157; Coverage: 100%)
Gene names: PH0574, alaXS
Sequence domains: Threonyl and Alanyl tRNA synthetase second additional domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 3 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P21
Unit cell:
a: 42.802Å b: 97.861Å c: 60.872Å
α: 90° β: 96.51° γ: 90°
R-values:
R R work R free
0.207 0.206 0.227
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Structural analyses clarify the complex control of mistranslation by tRNA synthetases.
Guo et al. (2012)
5 other articles

2 mentions without citation

Molecular basis of alanine discrimination in editing site.
Sokabe et al. (2005)
1 more