8ZYC

Cryo-EM structure of uropathogenic Escherichia coli CysK:CdiA:tRNA complex A

8ZYC の概要

• エントリーDOI: 10.2210/pdb8zyc/pdb
• EMDBエントリー: 60561
• 分子名称: Cysteine synthase A, tRNA nuclease CdiA, tRNAIleGAU, ... (4 entities in total)
• 機能のキーワード: rnase, complex, contact-dependent growth inhibition, toxin
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 119744.10

構造登録者

Feng, Z.,Yashiro, Y.,Tomita, K. (登録日: 2024-06-17, 公開日: 2024-08-21, 最終更新日: 2025-03-05)

主引用文献

Feng, Z.,Yashiro, Y.,Tomita, K.
Mechanism of activation of contact-dependent growth inhibition tRNase toxin by the amino acid biogenesis factor CysK in the bacterial competition system.
Nucleic Acids Res., 53:-, 2025

PubMed Abstract: Contact-dependent growth inhibition (CDI) is a bacterial competition mechanism, wherein the C-terminal toxin domain of CdiA protein (CdiA-CT) is transferred from one bacterium to another, impeding the growth of the toxin recipient. In uropathogenic Escherichia coli 536, CdiA-CT (CdiA-CTEC536) is a tRNA anticodon endonuclease that requires a cysteine biogenesis factor, CysK, for its activity. However, the mechanism underlying tRNA recognition and cleavage by CdiA-CTEC536 remains unresolved. Here, we present the cryo-EM structure of the CysK:CdiA-CTEC536:tRNA ternary complex. The interaction between CdiA-CTEC536 and CysK stabilizes the CdiA-CTEC536 structure and facilitates tRNA binding and the formation of the CdiA-CTEC536 catalytic core structure. The bottom-half of the tRNA interacts exclusively with CdiA-CTEC536 and the α-helices of CdiA-CTEC536 engage with the minor and major grooves of the bottom-half of tRNA, positioning the tRNA anticodon loop at the CdiA-CTEC536 catalytic site for tRNA cleavage. Thus, CysK serves as a platform facilitating the recognition and cleavage of substrate tRNAs by CdiA-CTEC536.

PubMed: 39228374
DOI: 10.1093/nar/gkae735

実験手法

ELECTRON MICROSCOPY (2.99 Å)