7PKT
Large subunit of the Chlamydomonas reinhardtii mitoribosome
This is a non-PDB format compatible entry.
Summary for 7PKT
| Entry DOI | 10.2210/pdb7pkt/pdb |
| Related | 7PKQ |
| EMDB information | 13477 13480 13481 13578 |
| Descriptor | Ribosomal_L2_C domain-containing protein, Mitochondrial ribosomal protein L17,bL17m, Mitochondrial ribosomal protein L19, ... (57 entities in total) |
| Functional Keywords | mitochondria, mitoribosome, alga, ribosome |
| Biological source | Chlamydomonas reinhardtii More |
| Total number of polymer chains | 54 |
| Total formula weight | 1926381.06 |
| Authors | Waltz, F.,Soufari, H.,Hashem, Y. (deposition date: 2021-08-26, release date: 2022-06-15, Last modification date: 2024-07-17) |
| Primary citation | Waltz, F.,Salinas-Giege, T.,Englmeier, R.,Meichel, H.,Soufari, H.,Kuhn, L.,Pfeffer, S.,Forster, F.,Engel, B.D.,Giege, P.,Drouard, L.,Hashem, Y. How to build a ribosome from RNA fragments in Chlamydomonas mitochondria. Nat Commun, 12:7176-7176, 2021 Cited by PubMed Abstract: Mitochondria are the powerhouse of eukaryotic cells. They possess their own gene expression machineries where highly divergent and specialized ribosomes, named hereafter mitoribosomes, translate the few essential messenger RNAs still encoded by mitochondrial genomes. Here, we present a biochemical and structural characterization of the mitoribosome in the model green alga Chlamydomonas reinhardtii, as well as a functional study of some of its specific components. Single particle cryo-electron microscopy resolves how the Chlamydomonas mitoribosome is assembled from 13 rRNA fragments encoded by separate non-contiguous gene pieces. Additional proteins, mainly OPR, PPR and mTERF helical repeat proteins, are found in Chlamydomonas mitoribosome, revealing the structure of an OPR protein in complex with its RNA binding partner. Targeted amiRNA silencing indicates that these ribosomal proteins are required for mitoribosome integrity. Finally, we use cryo-electron tomography to show that Chlamydomonas mitoribosomes are attached to the inner mitochondrial membrane via two contact points mediated by Chlamydomonas-specific proteins. Our study expands our understanding of mitoribosome diversity and the various strategies these specialized molecular machines adopt for membrane tethering. PubMed: 34887394DOI: 10.1038/s41467-021-27200-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
Download full validation report
