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Structure paper

TitleStructural basis for substrate recognition by the editing domain of isoleucyl-tRNA synthetase
Journal, issue, pagesJ. Mol. Biol., Vol. 359, Page 901-912, Year 2006
Publish dateMay 30, 2004 (structure data deposition date)
AuthorsFukunaga, R. / Yokoyama, S.
External linksJ. Mol. Biol. / PubMed:16697013
MethodsX-ray diffraction
Resolution1.6 - 1.7 Å
Structure data

PDB-1wk8:
Isoleucyl-tRNA synthetase editing domain complexed with the pre-transfer editing substrate analogue, Val-AMS
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-1wny:
Isoleucyl-tRNA synthetase editing domain
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

PDB-1wnz:
Isoleucyl-tRNA synthetase editing domain complexed with the post-transfer editing substrate analogue, Val-2AA
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

Chemicals

ChemComp-VMS:
5'O-[N-(L-VALYL)SULPHAMOYL]ADENOSINE

ChemComp-HOH:
WATER

ChemComp-2VA:
2'-(L-VALYL)AMINO-2'-DEOXYADENOSINE

Source
  • thermus thermophilus (bacteria)
KeywordsLIGASE / editing / cp1 / isoleucyl-trna synthetase / fidelity / thermus thermophilus / translation / amino acid / Structural Genomics / RIKEN Structural Genomics/Proteomics Initiative / RSGI / NPPSFA / National Project on Protein Structural and Functional Analyses

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