1GTR

STRUCTURAL BASIS OF ANTICODON LOOP RECOGNITION BY GLUTAMINYL-TRNA SYNTHETASE

1GTR の概要

• エントリーDOI: 10.2210/pdb1gtr/pdb
• 分子名称: RNA (74-MER), GLUTAMINYL-tRNA SYNTHETASE, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: complex (ligase-trna), complex (ligase-trna) complex, complex (ligase/trna)
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cytoplasm: P00962
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 87695.94

構造登録者

Rould, M.A.,Perona, J.J.,Steitz, T.A. (登録日: 1993-09-15, 公開日: 1995-02-07, 最終更新日: 2024-02-07)

主引用文献

Rould, M.A.,Perona, J.J.,Steitz, T.A.
Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase.
Nature, 352:213-218, 1991

PubMed Abstract: The refined crystal structure of Escherichia coli glutaminyl transfer RNA synthetase complexed with transfer RNA(Gln) and ATP reveals that the structure of the anticodon loop of the enzyme-bound tRNA(Gln) differs extensively from that of the known crystal structures of uncomplexed tRNA molecules. The anticodon stem is extended by two non-Watson-Crick base pairs, leaving the three anti-codon bases unpaired and splayed out to bind snugly into three separate complementary pockets in the protein. These interactions suggest that the entire anticodon loop provides essential sites for glutaminyl tRNA synthetase discrimination among tRNA molecules.

PubMed: 1857417
DOI: 10.1038/352213a0

実験手法

X-RAY DIFFRACTION (2.5 Å)