3amu

X-ray diffraction
3.1Å resolution

Crystal structure of the TiaS-tRNA(Ile2)-AMPCPP-agmatine complex

Released:
Source organism: Archaeoglobus fulgidus
Primary publication:
Structural basis of tRNA agmatinylation essential for AUA codon decoding.
Nat Struct Mol Biol 18 1275-80 (2011)
PMID: 22002223

Function and Biology Details

Reaction catalysed:
ATP + agmatine + (tRNA(Ile)(2))-cytidine(34) + H(2)O = (tRNA(Ile)(2))-2-agmatinylcytidine(34) + AMP + 2 phosphate
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-127932 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct RNA molecule
Macromolecules (2 distinct):
tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS Chain: A
Molecule details ›
Chain: A
Length: 440 amino acids
Theoretical weight: 50.54 KDa
Source organism: Archaeoglobus fulgidus
Expression system: Escherichia coli
UniProt:
  • Canonical: O28025 (Residues: 1-420; Coverage: 100%)
Gene names: AF_2259, tiaS
Sequence domains:
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
RNA (78-MER) Chain: B
Molecule details ›
Chain: B
Length: 78 nucleotides
Theoretical weight: 25.12 KDa
Source organism: Archaeoglobus fulgidus
Expression system: Not provided
Sequence domains: tRNA

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P3221
Unit cell:
a: 130.789Å b: 130.789Å c: 87.087Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.25 0.25 0.303
Expression systems:
  • Escherichia coli
  • Not provided