9KYF

Crystal structure of E.coli ac4C amidohydrolase YqfB

9KYF の概要

• エントリーDOI: 10.2210/pdb9kyf/pdb
• 分子名称: N(4)-acetylcytidine amidohydrolase, CALCIUM ION (3 entities in total)
• 機能のキーワード: n4-acetylcytidine, rna modification, amidohydrolase, hydrolase
• 由来する生物種: Escherichia coli BL21(DE3)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 23844.79

構造登録者

Guo, W.T.,Wu, B.X.,Meng, C.Y.,Wen, Y. (登録日: 2024-12-09, 公開日: 2025-08-20, 最終更新日: 2025-12-24)

主引用文献

Meng, C.,Shi, X.,Guo, W.,Jian, X.,Zhao, J.,Wen, Y.,Wang, R.,Li, Y.,Xu, S.,Chen, H.,Zhang, J.,Chen, M.,Chen, H.,Wu, B.
Structural analysis of ASCH domain-containing proteins and their implications for nucleotide processing.
Structure, 33:2095-2108.e5, 2025

PubMed Abstract: ASC-1 homology (ASCH) domain family proteins are believed to play essential roles in RNA metabolism, but detailed structural and functional information is limited. Research has shown that the E. coli enzyme YqfB, which contains an ASCH domain, has amidohydrolase activity, converting N-acetylcytidine (acC) RNA nucleoside into cytidine. Here, we present the crystal structures of EcYqfB both in its unbound state and bound to a substrate. Our analysis reveals how the substrate interacts with the enzyme, offering insights into its catalytic mechanism. In vivo experiments further show that deleting EcYqfB does not change overall acC levels across various RNA types, indicating that EcYqfB specifically functions in acC nucleoside metabolism. We also determined the structures of two homologous proteins: mouse EOLA1 and the human TRIP4-ASCH domain, highlighting differences in their substrate preferences. These findings offer important insights for future research into the structure and function of the ASCH domain protein family.

PubMed: 40939588
DOI: 10.1016/j.str.2025.08.015

実験手法

X-RAY DIFFRACTION (1.55 Å)