7AFA
Bacterial 30S ribosomal subunit assembly complex state F (head domain)
Summary for 7AFA
| Entry DOI | 10.2210/pdb7afa/pdb |
| EMDB information | 11758 |
| Descriptor | 16SrRNA (head domain of the 30S ribosome), MAGNESIUM ION, ZINC ION, ... (11 entities in total) |
| Functional Keywords | cryo-em, 30s biogenesis, ribosome assembly, rbfa, rsga, yjeq, rimp, ksga, rsma, ribosome |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 9 |
| Total formula weight | 634901.67 |
| Authors | Schedlbauer, A.,Iturrioz, I.,Ochoa-Lizarralde, B.,Kaminishi, T.,Diercks, T.,Capuni, R.,Astigarraga, E.,Gil-Carton, D.,Fucini, P.,Connell, S. (deposition date: 2020-09-19, release date: 2021-07-07, Last modification date: 2024-04-24) |
| Primary citation | Schedlbauer, A.,Iturrioz, I.,Ochoa-Lizarralde, B.,Diercks, T.,Lopez-Alonso, J.P.,Lavin, J.L.,Kaminishi, T.,Capuni, R.,Dhimole, N.,de Astigarraga, E.,Gil-Carton, D.,Fucini, P.,Connell, S.R. A conserved rRNA switch is central to decoding site maturation on the small ribosomal subunit. Sci Adv, 7:-, 2021 Cited by PubMed Abstract: While a structural description of the molecular mechanisms guiding ribosome assembly in eukaryotic systems is emerging, bacteria use an unrelated core set of assembly factors for which high-resolution structural information is still missing. To address this, we used single-particle cryo-electron microscopy to visualize the effects of bacterial ribosome assembly factors RimP, RbfA, RsmA, and RsgA on the conformational landscape of the 30 ribosomal subunit and obtained eight snapshots representing late steps in the folding of the decoding center. Analysis of these structures identifies a conserved secondary structure switch in the 16 ribosomal RNA central to decoding site maturation and suggests both a sequential order of action and molecular mechanisms for the assembly factors in coordinating and controlling this switch. Structural and mechanistic parallels between bacterial and eukaryotic systems indicate common folding features inherent to all ribosomes. PubMed: 34088665DOI: 10.1126/sciadv.abf7547 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.95 Å) |
Structure validation
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