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Structure paper

TitleInfluence of transfer RNA tertiary structure on aminoacylation efficiency by glutaminyl and cysteinyl-tRNA synthetases.
Journal, issue, pagesJ. Mol. Biol., Vol. 299, Page 431-446, Year 2000
Publish dateApr 17, 2000 (structure data deposition date)
AuthorsSherlin, L.D. / Bullock, T.L. / Newberry, K.J. / Lipman, R.S. / Hou, Y.M. / Beijer, B. / Sproat, B.S. / Perona, J.J.
External linksJ. Mol. Biol. / PubMed:10860750
MethodsX-ray diffraction
Resolution2.6 - 3.1 Å
Structure data

PDB-1euq:
CRYSTAL STRUCTURE OF GLUTAMINYL-TRNA SYNTHETASE COMPLEXED WITH A TRNA-GLN MUTANT AND AN ACTIVE-SITE INHIBITOR
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

PDB-1euy:
GLUTAMINYL-TRNA SYNTHETASE COMPLEXED WITH A TRNA MUTANT AND AN ACTIVE SITE INHIBITOR
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-QSI:
5'-O-[N-(L-GLUTAMINYL)-SULFAMOYL]ADENOSINE

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
Keywordsligase/RNA / TRNA SYNTHETASE / GLUTAMINE / TRNAGLN / E. COLI / RNA-PROTEIN COMPLEX / ligase-RNA COMPLEX / COMPLEX

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