6HIY
Cryo-EM structure of the Trypanosoma brucei mitochondrial ribosome - This entry contains the body of the small mitoribosomal subunit in complex with mt-IF-3
This is a non-PDB format compatible entry.
Summary for 6HIY
Entry DOI | 10.2210/pdb6hiy/pdb |
EMDB information | 0232 |
Descriptor | mS48, mS65, mS66, ... (45 entities in total) |
Functional Keywords | mitoribosome, translation, trypanosoma, small ribosomal subunit, 9s rrna, ribosomal protein, mitochondrial initiation factor if-3, ribosome |
Biological source | Trypanosoma brucei brucei More |
Total number of polymer chains | 41 |
Total formula weight | 1751904.27 |
Authors | Ramrath, D.J.F.,Niemann, M.,Leibundgut, M.,Bieri, P.,Prange, C.,Horn, E.K.,Leitner, A.,Boehringer, D.,Schneider, A.,Ban, N. (deposition date: 2018-08-31, release date: 2018-09-26, Last modification date: 2019-12-11) |
Primary citation | Ramrath, D.J.F.,Niemann, M.,Leibundgut, M.,Bieri, P.,Prange, C.,Horn, E.K.,Leitner, A.,Boehringer, D.,Schneider, A.,Ban, N. Evolutionary shift toward protein-based architecture in trypanosomal mitochondrial ribosomes. Science, 362:-, 2018 Cited by PubMed Abstract: Ribosomal RNA (rRNA) plays key functional and architectural roles in ribosomes. Using electron microscopy, we determined the atomic structure of a highly divergent ribosome found in mitochondria of , a unicellular parasite that causes sleeping sickness in humans. The trypanosomal mitoribosome features the smallest rRNAs and contains more proteins than all known ribosomes. The structure shows how the proteins have taken over the role of architectural scaffold from the rRNA: They form an autonomous outer shell that surrounds the entire particle and stabilizes and positions the functionally important regions of the rRNA. Our results also reveal the "minimal" set of conserved rRNA and protein components shared by all ribosomes that help us define the most essential functional elements. PubMed: 30213880DOI: 10.1126/science.aau7735 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.27 Å) |
Structure validation
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