6ZU5
Structure of the Paranosema locustae ribosome in complex with Lso2
This is a non-PDB format compatible entry.
Summary for 6ZU5
| Entry DOI | 10.2210/pdb6zu5/pdb |
| EMDB information | 11437 |
| Descriptor | 25S rRNA, eL31, eL6, ... (77 entities in total) |
| Functional Keywords | microsporidia, pathogen, ribosome, hibernation, genome compaction |
| Biological source | Paranosema locustae More |
| Total number of polymer chains | 74 |
| Total formula weight | 2628109.12 |
| Authors | Ehrenbolger, K.,Jespersen, N.,Sharma, H.,Sokolova, Y.Y.,Tokarev, Y.S.,Vossbrinck, C.R.,Barandun, J. (deposition date: 2020-07-21, release date: 2020-11-04, Last modification date: 2024-05-01) |
| Primary citation | Ehrenbolger, K.,Jespersen, N.,Sharma, H.,Sokolova, Y.Y.,Tokarev, Y.S.,Vossbrinck, C.R.,Barandun, J. Differences in structure and hibernation mechanism highlight diversification of the microsporidian ribosome. Plos Biol., 18:e3000958-e3000958, 2020 Cited by PubMed Abstract: Assembling and powering ribosomes are energy-intensive processes requiring fine-tuned cellular control mechanisms. In organisms operating under strict nutrient limitations, such as pathogenic microsporidia, conservation of energy via ribosomal hibernation and recycling is critical. The mechanisms by which hibernation is achieved in microsporidia, however, remain poorly understood. Here, we present the cryo-electron microscopy structure of the ribosome from Paranosema locustae spores, bound by the conserved eukaryotic hibernation and recycling factor Lso2. The microsporidian Lso2 homolog adopts a V-shaped conformation to bridge the mRNA decoding site and the large subunit tRNA binding sites, providing a reversible ribosome inactivation mechanism. Although microsporidian ribosomes are highly compacted, the P. locustae ribosome retains several rRNA segments absent in other microsporidia, and represents an intermediate state of rRNA reduction. In one case, the near complete reduction of an expansion segment has resulted in a single bound nucleotide, which may act as an architectural co-factor to stabilize a protein-protein interface. The presented structure highlights the reductive evolution in these emerging pathogens and sheds light on a conserved mechanism for eukaryotic ribosome hibernation. PubMed: 33125369DOI: 10.1371/journal.pbio.3000958 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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