6C0F
Yeast nucleolar pre-60S ribosomal subunit (state 2)
Summary for 6C0F
| Entry DOI | 10.2210/pdb6c0f/pdb |
| EMDB information | 7324 |
| Descriptor | Saccharomyces cerevisiae S288c 35S pre-ribosomal RNA miscRNA, 60S ribosomal protein L8-A, Ribosome production factor 1, ... (44 entities in total) |
| Functional Keywords | pre-60s, ribosome biogenesis, lsu processome, ribosome |
| Biological source | Saccharomyces cerevisiae BY4741 More |
| Total number of polymer chains | 43 |
| Total formula weight | 2443793.82 |
| Authors | Sanghai, Z.A.,Miller, L.,Barandun, J.,Hunziker, M.,Chaker-Margot, M.,Klinge, S. (deposition date: 2017-12-29, release date: 2018-03-14, Last modification date: 2024-10-23) |
| Primary citation | Sanghai, Z.A.,Miller, L.,Molloy, K.R.,Barandun, J.,Hunziker, M.,Chaker-Margot, M.,Wang, J.,Chait, B.T.,Klinge, S. Modular assembly of the nucleolar pre-60S ribosomal subunit. Nature, 556:126-129, 2018 Cited by PubMed Abstract: Early co-transcriptional events during eukaryotic ribosome assembly result in the formation of precursors of the small (40S) and large (60S) ribosomal subunits. A multitude of transient assembly factors regulate and chaperone the systematic folding of pre-ribosomal RNA subdomains. However, owing to a lack of structural information, the role of these factors during early nucleolar 60S assembly is not fully understood. Here we report cryo-electron microscopy (cryo-EM) reconstructions of the nucleolar pre-60S ribosomal subunit in different conformational states at resolutions of up to 3.4 Å. These reconstructions reveal how steric hindrance and molecular mimicry are used to prevent both premature folding states and binding of later factors. This is accomplished by the concerted activity of 21 ribosome assembly factors that stabilize and remodel pre-ribosomal RNA and ribosomal proteins. Among these factors, three Brix-domain proteins and their binding partners form a ring-like structure at ribosomal RNA (rRNA) domain boundaries to support the architecture of the maturing particle. The existence of mutually exclusive conformations of these pre-60S particles suggests that the formation of the polypeptide exit tunnel is achieved through different folding pathways during subsequent stages of ribosome assembly. These structures rationalize previous genetic and biochemical data and highlight the mechanisms that drive eukaryotic ribosome assembly in a unidirectional manner. PubMed: 29512650DOI: 10.1038/nature26156 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.7 Å) |
Structure validation
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