› 2aji

X-ray diffraction
3.2Å resolution

Crystal structure of the editing domain of E. coli leucyl-tRNA synthetase complexes with isoleucine

Released:
DOI: 10.2210/pdb2aji/pdb
PDB entry 2aji coloured by chain, front view.
PDB entry 2aji coloured by chain, side view.
PDB entry 2aji coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structures of the editing domain of Escherichia coli leucyl-tRNA synthetase and its complexes with Met and Ile reveal a lock-and-key mechanism for amino acid discrimination.
Liu Y, Liao J, Zhu B, Wang ED, Ding J
Biochem J 394 399-407 (2006)
PMID: 16277600

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139769 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Leucine--tRNA ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 196 amino acids
Theoretical weight: 21.29 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P07813 (Residues: 228-413; Coverage: 22%)
Gene names: JW0637, b0642, leuS
Sequence domains: Leucyl-tRNA synthetase, editing domain
Structure domains: Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P6322
Unit cell:
a: 112.487Å b: 112.487Å c: 135.023Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.234 0.232 0.284
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Organoboron Compounds: Effective Antibacterial and Antiparasitic Agents.
Coghi et al. (2021)
1 more

1 mention without citation

Crystal structures of the editing domain of Escherichia coli leucyl-tRNA synthetase and its complexes with Met and Ile reveal a lock-and-key mechanism for amino acid discrimination.
Liu et al. (2006)