Summary for 7OII
| Entry DOI | 10.2210/pdb7oii/pdb |
| EMDB information | 12930 |
| Descriptor | 23S rRNA, 50S ribosomal protein L13, 50S ribosomal protein L14, ... (57 entities in total) |
| Functional Keywords | cotranslational folding, cspa70-2, ribosome |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 55 |
| Total formula weight | 2158984.83 |
| Authors | Agirrezabala, X.,Samatova, E.,Macher, M.,Liutkute, M.,Gil-Carton, D.,Novacek, J.,Valle, M.,Rodnina, M.V. (deposition date: 2021-05-11, release date: 2022-01-19, Last modification date: 2025-03-12) |
| Primary citation | Agirrezabala, X.,Samatova, E.,Macher, M.,Liutkute, M.,Maiti, M.,Gil-Carton, D.,Novacek, J.,Valle, M.,Rodnina, M.V. A switch from alpha-helical to beta-strand conformation during co-translational protein folding. Embo J., 41:e109175-e109175, 2022 Cited by PubMed Abstract: Cellular proteins begin to fold as they emerge from the ribosome. The folding landscape of nascent chains is not only shaped by their amino acid sequence but also by the interactions with the ribosome. Here, we combine biophysical methods with cryo-EM structure determination to show that folding of a β-barrel protein begins with formation of a dynamic α-helix inside the ribosome. As the growing peptide reaches the end of the tunnel, the N-terminal part of the nascent chain refolds to a β-hairpin structure that remains dynamic until its release from the ribosome. Contacts with the ribosome and structure of the peptidyl transferase center depend on nascent chain conformation. These results indicate that proteins may start out as α-helices inside the tunnel and switch into their native folds only as they emerge from the ribosome. Moreover, the correlation of nascent chain conformations with reorientation of key residues of the ribosomal peptidyl-transferase center suggest that protein folding could modulate ribosome activity. PubMed: 34994471DOI: 10.15252/embj.2021109175 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
Download full validation report
