2hra

X-ray diffraction
1.9Å resolution

Crystal structures of the interacting domains from yeast glutamyl-tRNA synthetase and tRNA aminoacylation and nuclear export cofactor Arc1p reveal a novel function for an old fold

Released:

Function and Biology Details

Reaction catalysed:
ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate--tRNA ligase, cytoplasmic Chains: A, B
Molecule details ›
Chains: A, B
Length: 209 amino acids
Theoretical weight: 22.96 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P46655 (Residues: 1-191; Coverage: 27%)
Gene names: G0583, GUS1, HRB724, YGL245W
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1, SLS BEAMLINE X06SA
Spacegroup: C2221
Unit cell:
a: 51.959Å b: 107.113Å c: 167.865Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.214 0.262
Expression system: Escherichia coli