2e89

X-ray diffraction
2.5Å resolution

Crystal structure of Aquifex aeolicus TilS in a complex with ATP, Magnesium ion, and L-lysine

Released:

Function and Biology Details

Reaction catalysed:
(tRNA(Ile2))-cytidine(34) + L-lysine + ATP = (tRNA(Ile2))-lysidine(34) + AMP + diphosphate + H(2)O
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
tRNA(Ile)-lysidine synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 317 amino acids
Theoretical weight: 37.39 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O67728 (Residues: 1-317; Coverage: 100%)
Gene names: aq_1887, tilS
Sequence domains: PP-loop family
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P21
Unit cell:
a: 97.42Å b: 81.57Å c: 109.11Å
α: 90° β: 105.98° γ: 90°
R-values:
R R work R free
0.229 0.229 0.274
Expression system: Escherichia coli BL21(DE3)