5Y0Q

Crystal structure of BsTmcAL bound with AMPCPP

5Y0Q の概要

• エントリーDOI: 10.2210/pdb5y0q/pdb
• 分子名称: UPF0348 protein B4417_3650, DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER (3 entities in total)
• 機能のキーワード: acetate ligase, ligase
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 99184.15

構造登録者

Yamashita, S.,Tomita, K. (登録日: 2017-07-18, 公開日: 2018-07-18, 最終更新日: 2023-11-22)

主引用文献

Taniguchi, T.,Miyauchi, K.,Sakaguchi, Y.,Yamashita, S.,Soma, A.,Tomita, K.,Suzuki, T.
Acetate-dependent tRNA acetylation required for decoding fidelity in protein synthesis.
Nat. Chem. Biol., 14:1010-1020, 2018

PubMed Abstract: Modification of tRNA anticodons plays a critical role in ensuring accurate translation. N-acetylcytidine (acC) is present at the anticodon first position (position 34) of bacterial elongator tRNA. Herein, we identified Bacillus subtilis ylbM (renamed tmcAL) as a novel gene responsible for acC34 formation. Unlike general acetyltransferases that use acetyl-CoA, TmcAL activates an acetate ion to form acetyladenylate and then catalyzes acC34 formation through a mechanism similar to tRNA aminoacylation. The crystal structure of TmcAL with an ATP analog reveals the molecular basis of acC34 formation. The ΔtmcAL strain displayed a cold-sensitive phenotype and a strong genetic interaction with tilS that encodes the enzyme responsible for synthesizing lysidine (L) at position 34 of tRNA to facilitate AUA decoding. Mistranslation of the AUA codon as Met in the ΔtmcAL strain upon tilS repression suggests that acC34 modification of tRNA and L34 modification of tRNA act cooperatively to prevent misdecoding of the AUA codon.

PubMed: 30150682
DOI: 10.1038/s41589-018-0119-z

実験手法

X-RAY DIFFRACTION (2.1 Å)