› 3p0h

X-ray diffraction
3Å resolution

Leishmania major Tyrosyl-tRNA synthetase in complex with fisetin, cubic crystal form

Released:
DOI: 10.2210/pdb3p0h/pdb
PDB entry 3p0h coloured by chain, front view.
PDB entry 3p0h coloured by chain, side view.
PDB entry 3p0h coloured by chain, top view.
Source organism: Leishmania major
Primary publication:
The double-length tyrosyl-tRNA synthetase from the eukaryote Leishmania major forms an intrinsically asymmetric pseudo-dimer.
Larson ET, Kim JE, Castaneda LJ, Napuli AJ, Zhang Z, Fan E, Zucker FH, Verlinde CL, Buckner FS, Van Voorhis WC, Hol WG, Merritt EA
J Mol Biol 409 159-76 (2011)
PMID: 21420975

Function and Biology Details

Reaction catalysed: 
ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175709 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
tyrosine--tRNA ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 690 amino acids
Theoretical weight: 77.06 KDa
Source organism: Leishmania major
Expression system: Escherichia coli
UniProt:
  • Canonical: Q4QFJ7 (Residues: 1-682; Coverage: 100%)
Gene name: LMJF_14_1370
Sequence domains: tRNA synthetases class I (W and Y)
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand FSE 2 x FSE
1 modified residue:
Ligand MSE 42 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: I23
Unit cell:
a: 240.24Å b: 240.24Å c: 240.24Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.234 0.273
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Recent developments in drug discovery for leishmaniasis and human African trypanosomiasis.
Nagle et al. (2014)
5 more

7 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
6 more