9SFB

Structure at 2.7 A resolution of Thermus thermophilus tyrosyl-tRNA synthetase bound to a tRNA(Tyr)(GUA) transcript, the sulphamoyl analogue of tyrosyl-adenylate and pyrophosphate.

9SFB の概要

• エントリーDOI: 10.2210/pdb9sfb/pdb
• 分子名称: Tyrosine--tRNA ligase, Thermus thermophilus tRNATyr(GUC) transcript, PYROPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: aminoacyl-trna synthetase, ligase, trna, rna binding protein
• 由来する生物種: Thermus thermophilus HB27; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 77731.50

構造登録者

Cusack, S. (登録日: 2025-08-19, 公開日: 2025-09-03)

主引用文献

Yaremchuk, A.,Kriklivyi, I.,Tukalo, M.,Cusack, S.
Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition.
EMBO J, 21:3829-3840, 2002

PubMed Abstract: Bacterial tyrosyl-tRNA synthetases (TyrRS) possess a flexibly linked C-terminal domain of approximately 80 residues, which has hitherto been disordered in crystal structures of the enzyme. We have determined the structure of Thermus thermophilus TyrRS at 2.0 A resolution in a crystal form in which the C-terminal domain is ordered, and confirm that the fold is similar to part of the C-terminal domain of ribosomal protein S4. We have also determined the structure at 2.9 A resolution of the complex of T.thermophilus TyrRS with cognate tRNA(tyr)(G Psi A). In this structure, the C-terminal domain binds between the characteristic long variable arm of the tRNA and the anti-codon stem, thus recognizing the unique shape of the tRNA. The anticodon bases have a novel conformation with A-36 stacked on G-34, and both G-34 and Psi-35 are base-specifically recognized. The tRNA binds across the two subunits of the dimeric enzyme and, remarkably, the mode of recognition of the class I TyrRS for its cognate tRNA resembles that of a class II synthetase in being from the major groove side of the acceptor stem.

PubMed: 12110594
DOI: 10.1093/emboj/cdf373

実験手法

X-RAY DIFFRACTION (2.7 Å)