8OTK
Structure of ClpC Q11P N-terminal Domain
Summary for 8OTK
| Entry DOI | 10.2210/pdb8otk/pdb |
| Related | 8B3S |
| Descriptor | ATP-dependent Clp protease ATP-binding subunit ClpC / Negative regulator of tic competence clcC/mecB, PENTAETHYLENE GLYCOL, CARBONATE ION, ... (6 entities in total) |
| Functional Keywords | sporulation, chaperone |
| Biological source | Bacillus subtilis |
| Total number of polymer chains | 1 |
| Total formula weight | 18266.63 |
| Authors | Evans, N.J.,Isaacson, R.L.,Camp, A.H. (deposition date: 2023-04-21, release date: 2024-05-01, Last modification date: 2025-11-12) |
| Primary citation | Massoni, S.C.,Evans, N.J.,Hantke, I.,Fenton, C.,Torpey, J.H.,Collins, K.M.,Krysztofinska, E.M.,Muench, J.H.,Thapaliya, A.,Martinez-Lumbreras, S.,Hart Ferrell, S.,Slater, C.,Wang, X.,Fekade, R.,Obwar, S.,Yin, S.,Vazquez, A.,Prior, C.B.,Turgay, K.,Isaacson, R.L.,Camp, A.H. MdfA is a novel ClpC adaptor protein that functions in the developing Bacillus subtilis spore. Genes Dev., 39:510-523, 2025 Cited by PubMed Abstract: Bacterial protein degradation machinery consists of chaperone-protease complexes that play vital roles in bacterial growth and development and have sparked interest as novel antimicrobial targets. ClpC-ClpP (ClpCP) is one such chaperone-protease complex, recruited by adaptors to specific functions in the model bacterium and other Gram-positive bacteria, including the pathogens and Here we have identified a new ClpCP adaptor protein, MdfA (metabolic differentiation factor A; formerly YjbA), in a genetic screen for factors that help drive toward metabolic dormancy during spore formation. A knockout of stimulates gene expression in the developing spore, while aberrant expression of during vegetative growth is toxic. MdfA binds directly to ClpC to induce its oligomerization and ATPase activity, and this interaction is required for the in vivo effects of Finally, a cocrystal structure reveals that MdfA binds to the ClpC N-terminal domain at a location analogous to that on the ClpC1 protein where bactericidal cyclic peptides bind. Altogether, our data and that of an accompanying study by Riley and colleagues support a model in which MdfA induces ClpCP-mediated degradation of metabolic enzymes in the developing spore, helping drive it toward metabolic dormancy. PubMed: 40086879DOI: 10.1101/gad.352498.124 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.15 Å) |
Structure validation
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