1OBH

LEUCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH A PRE-TRANSFER EDITING SUBSTRATE ANALOGUE IN BOTH SYNTHETIC ACTIVE SITE AND EDITING SITE

1OBH の概要

• エントリーDOI: 10.2210/pdb1obh/pdb
• 関連するPDBエントリー: 1H3N 1JZQ 1JZS 1OBC
• 分子名称: LEUCYL-TRNA SYNTHETASE, SULFATE ION, MERCURY (II) ION, ... (6 entities in total)
• 機能のキーワード: synthetase, aminoacyl-trna synthetase, class i aminoacyl-trna synthetase, atp + l-leucine + trna (leu) -> amp + ppi l- leucyl-trna(leu)
• 由来する生物種: THERMUS THERMOPHILUS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 102874.05

構造登録者

Cusack, S.,Yaremchuk, A.,Tukalo, M. (登録日: 2003-01-31, 公開日: 2003-05-09, 最終更新日: 2024-11-20)

主引用文献

Lincecum, T.,Tukalo, M.,Yaremchuk, A.,Mursinna, R.,Williams, A.,Sproat, B.,Van Den Eynde, W.,Link, A.,Van Calenbergh, S.,Grotli, M.,Martinis, S.,Cusack, S.
Structural and Mechanistic Basis of Pre- and Posttransfer Editing by Leucyl-tRNA Synthetase
Mol.Cell, 11:951-, 2003

PubMed Abstract: The aminoacyl-tRNA synthetases link tRNAs with their cognate amino acid. In some cases, their fidelity relies on hydrolytic editing that destroys incorrectly activated amino acids or mischarged tRNAs. We present structures of leucyl-tRNA synthetase complexed with analogs of the distinct pre- and posttransfer editing substrates. The editing active site binds the two different substrates using a single amino acid discriminatory pocket while preserving the same mode of adenine recognition. This suggests a similar mechanism of hydrolysis for both editing substrates that depends on a key, completely conserved aspartic acid, which interacts with the alpha-amino group of the noncognate amino acid and positions both substrates for hydrolysis. Our results demonstrate the economy by which a single active site accommodates two distinct substrates in a proofreading process critical to the fidelity of protein synthesis.

PubMed: 12718881
DOI: 10.1016/S1097-2765(03)00098-4

実験手法

X-RAY DIFFRACTION (2.2 Å)