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TitleCrystal structures of the editing domain of Escherichia coli leucyl-tRNA synthetase and its complexes with Met and Ile reveal a lock-and-key mechanism for amino acid discrimination
Journal, issue, pagesBiochem. J., Vol. 394, Page 399-407, Year 2006
Publish dateAug 1, 2005 (structure data deposition date)
AuthorsLiu, Y. / Liao, J. / Zhu, B. / Wang, E.D. / Ding, J.
External linksBiochem. J. / PubMed:16277600
MethodsX-ray diffraction
Resolution2 - 3.2 Å
Structure data

PDB-2ajg:
Crystal structure of the editing domain of E. coli leucyl-tRNA synthetase
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-2ajh:
Crystal structure of the editing domain of E. coli leucyl-tRNA synthetase complexes with methionine
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-2aji:
Crystal structure of the editing domain of E. coli leucyl-tRNA synthetase complexes with isoleucine
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-MET:
METHIONINE

ChemComp-ILE:
ISOLEUCINE

Source
  • escherichia coli (E. coli)
KeywordsLIGASE / editing domain / leucyl-tRNA synthetase

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