8S32
GroEL with bound GroTAC peptide
Summary for 8S32
| Entry DOI | 10.2210/pdb8s32/pdb |
| EMDB information | 19687 |
| Descriptor | Chaperonin GroEL, GroTAC (2 entities in total) |
| Functional Keywords | groel, grotac, protac, degrader, complex, chaperone |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 28 |
| Total formula weight | 847958.92 |
| Authors | Wroblewski, K.,Izert-Nowakowska, M.A.,Goral, T.K.,Klimecka, M.M.,Kmiecik, S.,Gorna, M.W. (deposition date: 2024-02-19, release date: 2024-02-28, Last modification date: 2025-09-10) |
| Primary citation | 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 Cited by 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: 40562793DOI: 10.1038/s44319-025-00510-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.45 Å) |
Structure validation
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