9R3A
Structure of Stalled Beta-Galactosidase 70S Ribosome Nascent Chain
This is a non-PDB format compatible entry.
Summary for 9R3A
| Entry DOI | 10.2210/pdb9r3a/pdb |
| EMDB information | 53553 |
| Descriptor | Large ribosomal subunit protein bL33, Small ribosomal subunit protein uS4, Small ribosomal subunit protein uS5, ... (60 entities in total) |
| Functional Keywords | translation, co-translational folding, nascent chain, protein folding, ribosome |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 56 |
| Total formula weight | 2209160.33 |
| Authors | |
| Primary citation | Roeselova, A.,Shivakumaraswamy, S.,Jurkeviciute, G.,He, J.Z.,Auburger, J.,Schmitt, J.L.,Kramer, G.,Bukau, B.,Enchev, R.I.,Balchin, D. The ribosome synchronizes folding and assembly to promote oligomeric protein biogenesis. Mol.Cell, 2026 Cited by PubMed Abstract: Natural proteins often form intricate multidomain, oligomeric architectures. This presents a prima facie challenge to cellular homeostasis, as topologically complex proteins seldom refold efficiently in vitro. Here, we show that the efficient folding and assembly of the five-domain homotetramer β-galactosidase is obligatorily coupled to its synthesis on the ribosome, and we define the underlying mechanisms. During refolding from a denaturant, maturation of the catalytic domain is frustrated. Assembly outpaces monomer folding, and non-native oligomers accumulate. Efficient de novo folding is characterized by segmental domain folding, shaped by the binding of a nascent amphipathic helix to a cryptic pocket on uL23 on the ribosome surface. Homomer assembly also initiates cotranslationally via recruitment of a full-length subunit to the nascent polypeptide, and the failure to do so results in misassembly. Our results reveal how the ribosome can dictate the timing of folding and assembly to enable efficient biogenesis of a topologically complex protein. PubMed: 41558483DOI: 10.1016/j.molcel.2025.12.022 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.86 Å) |
Structure validation
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