6W7M
30S-Inactive-high-Mg2+ + carbon layer
Summary for 6W7M
| Entry DOI | 10.2210/pdb6w7m/pdb |
| Related | 6W6K 6W77 |
| EMDB information | 21558 21569 21570 21571 |
| Descriptor | 16S rRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (20 entities in total) |
| Functional Keywords | 30s subunit, conformations, inactive, activated, ribosome |
| Biological source | Escherichia coli (strain K12) More |
| Total number of polymer chains | 20 |
| Total formula weight | 780984.04 |
| Authors | Jahagirdar, D.,Jha, V.,Basu, B.,Gomez-Blanco, J.,Vargas, J.,Ortega, J. (deposition date: 2020-03-19, release date: 2020-10-21, Last modification date: 2024-03-06) |
| Primary citation | Jahagirdar, D.,Jha, V.,Basu, K.,Gomez-Blanco, J.,Vargas, J.,Ortega, J. Alternative conformations and motions adopted by 30S ribosomal subunits visualized by cryo-electron microscopy. Rna, 26:2017-2030, 2020 Cited by PubMed Abstract: It is only after recent advances in cryo-electron microscopy that it is now possible to describe at high-resolution structures of large macromolecules that do not crystalize. Purified 30S subunits interconvert between an "active" and "inactive" conformation. The active conformation was described by crystallography in the early 2000s, but the structure of the inactive form at high resolution remains unsolved. Here we used cryo-electron microscopy to obtain the structure of the inactive conformation of the 30S subunit to 3.6 Å resolution and study its motions. In the inactive conformation, an alternative base-pairing of three nucleotides causes the region of helix 44, forming the decoding center to adopt an unlatched conformation and the 3' end of the 16S rRNA positions similarly to the mRNA during translation. Incubation of inactive 30S subunits at 42°C reverts these structural changes. The air-water interface to which ribosome subunits are exposed during sample preparation also peel off some ribosomal proteins. Extended exposures to low magnesium concentrations make the ribosomal particles more susceptible to the air-water interface causing the unfolding of large rRNA structural domains. Overall, this study provides new insights about the conformational space explored by the 30S ribosomal subunit when the ribosomal particles are free in solution. PubMed: 32989043DOI: 10.1261/rna.075846.120 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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