6FU8
uL23 beta hairpin loop deletion of E.coli ribosome
Summary for 6FU8
| Entry DOI | 10.2210/pdb6fu8/pdb |
| EMDB information | 4319 |
| Descriptor | 50S ribosomal protein L23 (1 entity in total) |
| Functional Keywords | ul23, loop deletion, ribosomal tunnel, ribosomal protein |
| Biological source | Escherichia coli O157:H7 |
| Total number of polymer chains | 1 |
| Total formula weight | 9324.00 |
| Authors | Kudva, R.,von Heijne, G.,Carroni, M. (deposition date: 2018-02-26, release date: 2018-12-05, Last modification date: 2024-05-15) |
| Primary citation | Kudva, R.,Tian, P.,Pardo-Avila, F.,Carroni, M.,Best, R.B.,Bernstein, H.D.,von Heijne, G. The shape of the bacterial ribosome exit tunnel affects cotranslational protein folding. Elife, 7:-, 2018 Cited by PubMed Abstract: The ribosome exit tunnel can accommodate small folded proteins, while larger ones fold outside. It remains unclear, however, to what extent the geometry of the tunnel influences protein folding. Here, using ribosomes with deletions in loops in proteins uL23 and uL24 that protrude into the tunnel, we investigate how tunnel geometry determines where proteins of different sizes fold. We find that a 29-residue zinc-finger domain normally folding close to the uL23 loop folds deeper in the tunnel in uL23 Δloop ribosomes, while two ~ 100 residue proteins normally folding close to the uL24 loop near the tunnel exit port fold at deeper locations in uL24 Δloop ribosomes, in good agreement with results obtained by coarse-grained molecular dynamics simulations. This supports the idea that cotranslational folding commences once a protein domain reaches a location in the exit tunnel where there is sufficient space to house the folded structure. PubMed: 30475203DOI: 10.7554/eLife.36326 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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