› 6iy6

X-ray diffraction
3.6Å resolution

Crystal structure of human cytosolic aspartyl-tRNA synthetase (DRS) in complex with glutathion-S transferase (GST) domains from Aminoacyl tRNA synthase complex-interacting multifunctional protein 2 (AIMP2) and glutamyl-prolyl-tRNA synthetase (EPRS)

Released:
DOI: 10.2210/pdb6iy6/pdb
PDB entry 6iy6 coloured by chain, front view.
PDB entry 6iy6 coloured by chain, side view.
PDB entry 6iy6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The DRS-AIMP2-EPRS subcomplex acts as a pivot in the multi-tRNA synthetase complex.
Hahn H, Park SH, Kim HJ, Kim S, Han BW
OpenAccess logo IUCrJ 6 958-967 (2019)
PMID: 31576228

Function and Biology Details

Reactions catalysed: 
ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp)
ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro)
ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
PDBe Complex ID:
PDB-CPX-139774 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Aspartate--tRNA ligase, cytoplasmic Chains: A, B, G, H
Molecule details ›
Chains: A, B, G, H
Length: 502 amino acids
Theoretical weight: 57.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P14868 (Residues: 21-501; Coverage: 96%)
  • Best match: P14868-2 (Residues: 1-401)
Gene names: DARS, DARS1, PIG40
Sequence domains:
Aminoacyl tRNA synthase complex-interacting multifunctional protein 2 Chains: C, D, I, J
Molecule details ›
Chains: C, D, I, J
Length: 215 amino acids
Theoretical weight: 24.17 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13155 (Residues: 115-320; Coverage: 64%)
  • Best match: Q13155-2 (Residues: 45-251)
Gene names: AIMP2, JTV1, PRO0992
Sequence domains:
Bifunctional glutamate/proline--tRNA ligase Chains: E, F, K, L
Molecule details ›
Chains: E, F, K, L
Length: 165 amino acids
Theoretical weight: 18.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P07814 (Residues: 1-157; Coverage: 10%)
Gene names: EPRS, EPRS1, GLNS, PARS, PIG32, QARS, QPRS
Sequence domains: Nuclear-export cofactor Arc1p

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand PO4 17 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: P61
Unit cell:
a: 108.068Å b: 108.068Å c: 815.642Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.239 0.237 0.275
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Roles of aminoacyl-tRNA synthetase-interacting multi-functional proteins in physiology and cancer.
Zhou et al. (2020)
1 more

1 mention without citation

The DRS-AIMP2-EPRS subcomplex acts as a pivot in the multi-tRNA synthetase complex.
Hahn et al. (2019)