2ZZK

Crystal structure of tRNA wybutosine synthesizing enzyme TYW4

2ZZK の概要

• エントリーDOI: 10.2210/pdb2zzk/pdb
• 関連するPDBエントリー: 2ZW9 2ZWA
• 分子名称: Leucine carboxyl methyltransferase 2, CITRIC ACID, TETRAETHYLENE GLYCOL, ... (4 entities in total)
• 機能のキーワード: trna modification, transferase
• 由来する生物種: Saccharomyces cerevisiae
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 159063.72

構造登録者

Suzuki, Y.,Noma, A.,Suzuki, T.,Ishitani, R.,Nureki, O. (登録日: 2009-02-17, 公開日: 2009-06-02, 最終更新日: 2024-03-13)

主引用文献

Suzuki, Y.,Noma, A.,Suzuki, T.,Ishitani, R.,Nureki, O.
Structural basis of tRNA modification with CO2 fixation and methylation by wybutosine synthesizing enzyme TYW4.
Nucleic Acids Res., 37:2910-2925, 2009

PubMed Abstract: Wybutosine (yW), one of the most complicated modified nucleosides, is found in the anticodon loop of eukaryotic phenylalanine tRNA. This hypermodified nucleoside ensures correct codon recognition by stabilizing codon-anticodon pairings during the decoding process in the ribosome. TYW4 is an S-adenosylmethionine (SAM)-dependent enzyme that catalyzes the final step of yW biosynthesis, methylation and methoxycarbonylation. However, the structural basis for the catalytic mechanism by TYW4, and especially that for the methoxycarbonylation, have remained elusive. Here we report the apo and cofactor-bound crystal structures of yeast TYW4. The structures revealed that the C-terminal domain folds into a beta-propeller structure, forming part of the binding pocket for the target nucleoside. A comparison of the apo, SAM-bound, and S-adenosylhomocysteine-bound structures of TYW4 revealed a drastic structural change upon cofactor binding, which may sequester solvent from the catalytic site during the reaction and facilitate product release after the reaction. In conjunction with the functional analysis, our results suggest that TYW4 catalyzes both methylation and methoxycarbonylation at a single catalytic site, and in the latter reaction, the methoxycarbonyl group is formed through the fixation of carbon dioxide.

PubMed: 19287006
DOI: 10.1093/nar/gkp158

実験手法

X-RAY DIFFRACTION (2.706 Å)