› 1j09

X-ray diffraction
1.8Å resolution

Crystal structure of Thermus thermophilus glutamyl-tRNA synthetase complexed with ATP and Glu

Released:
DOI: 10.2210/pdb1j09/pdb
PDB entry 1j09 coloured by chain, front view.
PDB entry 1j09 coloured by chain, side view.
PDB entry 1j09 coloured by chain, top view.
Source organism: Thermus thermophilus
Primary publication:
ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding.
Sekine S, Nureki O, Dubois DY, Bernier S, Chênevert R, Lapointe J, Vassylyev DG, Yokoyama S
EMBO J 22 676-88 (2003)
PMID: 12554668

Function and Biology Details

Reaction catalysed: 
ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150904 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate--tRNA ligase Chain: A
Molecule details ›
Chain: A
Length: 468 amino acids
Theoretical weight: 53.99 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P27000 (Residues: 1-468; Coverage: 100%)
Gene names: TTHA0438, gltX
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 1 x MG
Ligand GLU 1 x GLU
Ligand ATP 1 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P212121
Unit cell:
a: 81.92Å b: 82.62Å c: 83.11Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.199 0.227
Expression system: Escherichia coli BL21(DE3)

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Citations

6 review citations

Conformational dynamics in the Acyl-CoA synthetases, adenylation domains of non-ribosomal peptide synthetases, and firefly luciferase.
Gulick AM. (2009)
5 more

13 mentions without citation

Personalized Medicine in Mitochondrial Health and Disease: Molecular Basis of Therapeutic Approaches Based on Nutritional Supplements and Their Analogs.
Tragni et al. (2022)
12 more