1QU2

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

Summary for 1QU2

• Entry DOI: 10.2210/pdb1qu2/pdb
• Descriptor: ISOLEUCYL-TRNA, ISOLEUCYL-TRNA SYNTHETASE, POTASSIUM ION, ... (7 entities in total)
• Functional Keywords: protein-rna complex, metal ions, editing trna synthetase, double-sieve, ligase-rna complex, ligase/rna
• Biological source: Staphylococcus aureus; More
• Cellular location: Cytoplasm: P41972
• Total number of polymer chains: 2
• Total formula weight: 130207.31

Authors

Silvian, L.F.,Wang, J.,Steitz, T.A. (deposition date: 1999-07-06, release date: 1999-08-31, Last modification date: 2023-08-23)

Primary citation

Silvian, L.F.,Wang, J.,Steitz, T.A.
Insights into editing from an ile-tRNA synthetase structure with tRNAile and mupirocin.
Science, 285:1074-1077, 1999

PubMed Abstract: 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.

PubMed: 10446055
DOI: 10.1126/science.285.5430.1074

Experimental method

X-RAY DIFFRACTION (2.2 Å)