8S32

GroEL with bound GroTAC peptide

8S32 の概要

• エントリーDOI: 10.2210/pdb8s32/pdb
• EMDBエントリー: 19687
• 分子名称: Chaperonin GroEL, GroTAC (2 entities in total)
• 機能のキーワード: groel, grotac, protac, degrader, complex, chaperone
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 28
• 化学式量合計: 847958.92

構造登録者

Wroblewski, K.,Izert-Nowakowska, M.A.,Goral, T.K.,Klimecka, M.M.,Kmiecik, S.,Gorna, M.W. (登録日: 2024-02-19, 公開日: 2024-02-28, 最終更新日: 2025-09-10)

主引用文献

Izert-Nowakowska, M.A.,Klimecka, M.M.,Antosiewicz, A.,Wroblewski, K.,Kowalski, J.J.,Bandyra, K.J.,Goral, T.,Kmiecik, S.,Serwa, R.A.,Gorna, M.W.
Targeted protein degradation in Escherichia coli using CLIPPERs.
Embo Rep., 26:3994-4016, 2025

PubMed Abstract: New, universal tools for targeted protein degradation in bacteria can help to accelerate protein function studies and antimicrobial research. We describe a new method for degrading bacterial proteins using plasmid-encoded degrader peptides which deliver target proteins for degradation by a highly conserved ClpXP protease. We demonstrate the mode of action of the degraders on a challenging essential target, GroEL. The studies in bacteria are complemented by in vitro binding and structural studies. Expression of degrader peptides results in a temperature-dependent growth inhibition and depletion of GroEL levels over time. The reduction of GroEL levels is accompanied by dramatic proteome alterations. The presented method offers a new alternative approach for regulating protein levels in bacteria without genomic modifications or tag fusions. Our studies demonstrate that ClpXP is an attractive protease for the future use in bacterial-targeted protein degradation.

PubMed: 40562793
DOI: 10.1038/s44319-025-00510-9

実験手法

ELECTRON MICROSCOPY (2.45 Å)