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1qu2

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1qu2, resolution 2.20Å ()
Ligands: , , ,
Activity: Isoleucine--tRNA ligase, with EC number 6.1.1.5
Domains: Anticodon_1, zf-FPG_IleRS, IleRS_core, ileS
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



INSIGHTS INTO EDITING FROM AN ILE-TRNA SYNTHETASE STRUCTURE WITH TRNA(ILE) AND MUPIROCIN

Publication Abstract from PubMed

Isoleucyl-transfer RNA (tRNA) synthetase (IleRS) joins Ile to tRNA(Ile) at its synthetic active site and hydrolyzes incorrectly acylated amino acids at its editing active site. The 2.2 angstrom resolution crystal structure of Staphylococcus aureus IleRS complexed with tRNA(Ile) and Mupirocin shows the acceptor strand of the tRNA(Ile) in the continuously stacked, A-form conformation with the 3' terminal nucleotide in the editing active site. To position the 3' terminus in the synthetic active site, the acceptor strand must adopt the hairpinned conformation seen in tRNA(Gln) complexed with its synthetase. The amino acid editing activity of the IleRS may result from the incorrect products shuttling between the synthetic and editing active sites, which is reminiscent of the editing mechanism of DNA polymerases.

Insights into editing from an ile-tRNA synthetase structure with tRNAile and mupirocin., Silvian LF, Wang J, Steitz TA, Science. 1999 Aug 13;285(5430):1074-7. PMID:10446055

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1QU2 is a 2 chains structure of sequences from Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

  • Silvian LF, Wang J, Steitz TA. Insights into editing from an ile-tRNA synthetase structure with tRNAile and mupirocin. Science. 1999 Aug 13;285(5430):1074-7. PMID:10446055

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