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Structure paper

TitleA Succession of Substrate Induced Conformational Changes Ensures the Amino Acid Specificity of Thermus Thermophilus Prolyl-tRNA Synthetase: Comparison with Histidyl-tRNA Synthetase
Journal, issue, pagesJ. Mol. Biol., Vol. 309, Page 989-, Year 2001
Publish dateMay 13, 2001 (structure data deposition date)
AuthorsYaremchuk, A. / Tukalo, M. / Grotli, M. / Cusack, S.
External linksJ. Mol. Biol. / PubMed:11399074
MethodsX-ray diffraction
Resolution2.4 - 3 Å
Structure data

PDB-1h4q:
Prolyl-tRNA synthetase from Thermus thermophilus complexed with tRNApro(CGG), ATP and prolinol
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-1h4s:
Prolyl-tRNA synthetase from Thermus thermophilus complexed with tRNApro(CGG) and a prolyl-adenylate analogue
Method: X-RAY DIFFRACTION / Resolution: 2.85 Å

PDB-1h4t:
Prolyl-tRNA synthetase from Thermus thermophilus complexed with L-proline
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

PDB-1h4v:
HISTIDYL-TRNA SYNTHETASE from Thermus Thermophilus (ligand free)
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-1hc7:
Prolyl-tRNA synthetase from Thermus thermophilus
Method: X-RAY DIFFRACTION / Resolution: 2.43 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-ZN:
Unknown entry

ChemComp-PRI:
PYRROLIDINE-2-CARBALDEHYDE

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-P5A:
'5'-O-(N-(L-PROLYL)-SULFAMOYL)ADENOSINE

ChemComp-PRO:
PROLINE

Source
  • thermus thermophilus (bacteria)
KeywordsAMINOACYL-TRNA SYNTHETASE / ATP + L-PROLINE + TRNA(PRO) AMP + PPI + L-PROLYL-TRNA(PRO) / CLASS II AMINOACYL-TRNA SYNTHETASE / TRNA SYNTHETASE / CLASS IIA AMINOACYL-TRNA SYNTHETASE / ATP + L-HISTIDINE TRNA(HIS)-> AMP + PPI + L-HISTIDYL-TRNA(HIS)

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