6Z1P
Structure of the mitochondrial ribosome from Tetrahymena thermophila
This is a non-PDB format compatible entry.
Summary for 6Z1P
| Entry DOI | 10.2210/pdb6z1p/pdb |
| EMDB information | 11032 11033 11034 11035 11036 11037 11038 |
| Descriptor | LSU rRNA_1, bL7/12m, MAGNESIUM ION, ... (103 entities in total) |
| Functional Keywords | mitochondrial ribosome, ribosome, mitochondria, ciliate, tetrahymena |
| Biological source | Tetrahymena thermophila (strain SB210) More |
| Total number of polymer chains | 99 |
| Total formula weight | 4578607.38 |
| Authors | Tobiasson, V.,Amunts, A. (deposition date: 2020-05-14, release date: 2020-06-24, Last modification date: 2024-05-22) |
| Primary citation | Tobiasson, V.,Amunts, A. Ciliate mitoribosome illuminates evolutionary steps of mitochondrial translation. Elife, 9:-, 2020 Cited by PubMed Abstract: To understand the steps involved in the evolution of translation, we used , a ciliate with high coding capacity of the mitochondrial genome, as the model organism and characterized its mitochondrial ribosome (mitoribosome) using cryo-EM. The structure of the mitoribosome reveals an assembly of 94-ribosomal proteins and four-rRNAs with an additional protein mass of ~700 kDa on the small subunit, while the large subunit lacks 5S rRNA. The structure also shows that the small subunit head is constrained, tRNA binding sites are formed by mitochondria-specific protein elements, conserved protein bS1 is excluded, and bacterial RNA polymerase binding site is blocked. We provide evidence for anintrinsic protein targeting system through visualization of mitochondria-specific mL105 by the exit tunnel that would facilitate the recruitment of a nascent polypeptide. Functional protein uS3m is encoded by three complementary genes from the nucleus and mitochondrion, establishing a link between genetic drift and mitochondrial translation. Finally, we reannotated nine open reading frames in the mitochondrial genome that code for mitoribosomal proteins. PubMed: 32553108DOI: 10.7554/eLife.59264 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.7 Å) |
Structure validation
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