9GUL
Structure of FLuc-XBP1u+ stalled human 60S ribosome nascent chain complex
This is a non-PDB format compatible entry.
Summary for 9GUL
| Entry DOI | 10.2210/pdb9gul/pdb |
| EMDB information | 51611 |
| Descriptor | Stalled NC, Large ribosomal subunit protein eL6, Large ribosomal subunit protein uL30, ... (49 entities in total) |
| Functional Keywords | ribosome-nascent chain, translation, luciferase, folding |
| Biological source | Photinus pyralis More |
| Total number of polymer chains | 46 |
| Total formula weight | 2593890.13 |
| Authors | Voisin, T.B.,Pellowe, G.A.,Balchin, D. (deposition date: 2024-09-19, release date: 2025-09-24, Last modification date: 2025-11-26) |
| Primary citation | Pellowe, G.A.,Voisin, T.B.,Karpauskaite, L.,Maslen, S.L.,Roeselova, A.,Skehel, J.M.,Roustan, C.,George, R.,Nans, A.,Kjaer, S.,Taylor, I.A.,Balchin, D. The human ribosome modulates multidomain protein biogenesis by delaying cotranslational domain docking. Nat.Struct.Mol.Biol., 32:2296-2307, 2025 Cited by PubMed Abstract: Proteins with multiple domains are intrinsically prone to misfold, yet fold efficiently during their synthesis on the ribosome. This is especially important in eukaryotes, where multidomain proteins predominate. Here we sought to understand how multidomain protein folding is modulated by the eukaryotic ribosome. We used hydrogen-deuterium exchange mass spectrometry and cryo-electron microscopy to characterize the structure and dynamics of partially synthesized intermediates of a model multidomain protein. We find that nascent subdomains fold progressively during synthesis on the human ribosome, templated by interactions across domain interfaces. The conformational ensemble of the nascent chain is tuned by its unstructured C-terminal segments, which keep interfaces between folded domains in dynamic equilibrium until translation termination. This contrasts with the bacterial ribosome, on which domain interfaces form early and remain stable during synthesis. Delayed domain docking may avoid interdomain misfolding to promote the maturation of multidomain proteins in eukaryotes. PubMed: 40973728DOI: 10.1038/s41594-025-01676-5 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.2 Å) |
Structure validation
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