1QU2

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

1QU2 の概要

• エントリーDOI: 10.2210/pdb1qu2/pdb
• 分子名称: ISOLEUCYL-TRNA, ISOLEUCYL-TRNA SYNTHETASE, POTASSIUM ION, ... (7 entities in total)
• 機能のキーワード: protein-rna complex, metal ions, editing trna synthetase, double-sieve, ligase-rna complex, ligase/rna
• 由来する生物種: Staphylococcus aureus; 詳細
• 細胞内の位置: Cytoplasm: P41972
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 130207.31

構造登録者

Silvian, L.F.,Wang, J.,Steitz, T.A. (登録日: 1999-07-06, 公開日: 1999-08-31, 最終更新日: 2023-08-23)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.2 Å)