› 1fyj

Solution NMR

SOLUTION STRUCTURE OF MULTI-FUNCTIONAL PEPTIDE MOTIF-1 PRESENT IN HUMAN GLUTAMYL-PROLYL TRNA SYNTHETASE (EPRS).

Released:
DOI: 10.2210/pdb1fyj/pdb
PDB entry 1fyj coloured by chain, ensemble of 20 models, front view.
PDB entry 1fyj coloured by chain, ensemble of 20 models, side view.
PDB entry 1fyj coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase: identification of RNA-binding residues and functional implications for tandem repeats.
Jeong EJ, Hwang GS, Kim KH, Kim MJ, Kim S, Kim KS
Biochemistry 39 15775-82 (2000)
PMID: 11123902

Function and Biology Details

Reactions catalysed: 
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:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139771 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional glutamate/proline--tRNA ligase Chain: A
Molecule details ›
Chain: A
Length: 57 amino acids
Theoretical weight: 6.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P07814 (Residues: 749-805; Coverage: 4%)
Gene names: EPRS, EPRS1, GLNS, PARS, PIG32, QARS, QPRS
Sequence domains: WHEP-TRS domain
Structure domains: S15/NS1, RNA-binding

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry simulated annealing
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Functional expansion of aminoacyl-tRNA synthetases and their interacting factors: new perspectives on housekeepers.
Park et al. (2005)
7 more

5 mentions without citation

Gentamicin binds to the megalin receptor as a competitive inhibitor using the common ligand binding motif of complement type repeats: insight from the nmr structure of the 10th complement type repeat domain alone and in complex with gentamicin.
Dagil et al. (2013)
4 more