› 1wnz

X-ray diffraction
1.7Å resolution

Isoleucyl-tRNA synthetase editing domain complexed with the post-transfer editing substrate analogue, Val-2AA

Released:
DOI: 10.2210/pdb1wnz/pdb
PDB entry 1wnz coloured by chain, front view.
PDB entry 1wnz coloured by chain, side view.
PDB entry 1wnz coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
Structural basis for substrate recognition by the editing domain of isoleucyl-tRNA synthetase.
Fukunaga R, Yokoyama S
J Mol Biol 359 901-12 (2006)
PMID: 16697013

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157524 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isoleucine--tRNA ligase Chain: A
Molecule details ›
Chain: A
Length: 186 amino acids
Theoretical weight: 20.63 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P56690 (Residues: 200-385; Coverage: 18%)
Gene names: TTHA1067, ileS
Sequence domains: tRNA synthetases class I (I, L, M and V)
Structure domains: Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P4122
Unit cell:
a: 72.594Å b: 72.594Å c: 83.683Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.21 0.257
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Aminoacyl-tRNA synthesis and translational quality control.
Ling et al. (2009)
5 more

1 mention without citation

Negative catalysis by the editing domain of class I aminoacyl-tRNA synthetases.
Zivkovic et al. (2022)