6Z6L
Cryo-EM structure of human CCDC124 bound to 80S ribosomes
This is a non-PDB format compatible entry.
Summary for 6Z6L
Entry DOI | 10.2210/pdb6z6l/pdb |
EMDB information | 11098 |
Descriptor | 28S rRNA, 60S ribosomal protein L7a, 60S ribosomal protein L9, ... (85 entities in total) |
Functional Keywords | ribosome, hibernation |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 83 |
Total formula weight | 3905298.75 |
Authors | Wells, J.N.,Buschauer, R.,Mackens-Kiani, T.,Best, K.,Kratzat, H.,Berninghausen, O.,Becker, T.,Cheng, J.,Beckmann, R. (deposition date: 2020-05-28, release date: 2020-07-29, Last modification date: 2024-05-22) |
Primary citation | Wells, J.N.,Buschauer, R.,Mackens-Kiani, T.,Best, K.,Kratzat, H.,Berninghausen, O.,Becker, T.,Gilbert, W.,Cheng, J.,Beckmann, R. Structure and function of yeast Lso2 and human CCDC124 bound to hibernating ribosomes. Plos Biol., 18:e3000780-e3000780, 2020 Cited by PubMed Abstract: Cells adjust to nutrient deprivation by reversible translational shutdown. This is accompanied by maintaining inactive ribosomes in a hibernation state, in which they are bound by proteins with inhibitory and protective functions. In eukaryotes, such a function was attributed to suppressor of target of Myb protein 1 (Stm1; SERPINE1 mRNA-binding protein 1 [SERBP1] in mammals), and recently, late-annotated short open reading frame 2 (Lso2; coiled-coil domain containing short open reading frame 124 [CCDC124] in mammals) was found to be involved in translational recovery after starvation from stationary phase. Here, we present cryo-electron microscopy (cryo-EM) structures of translationally inactive yeast and human ribosomes. We found Lso2/CCDC124 accumulating on idle ribosomes in the nonrotated state, in contrast to Stm1/SERBP1-bound ribosomes, which display a rotated state. Lso2/CCDC124 bridges the decoding sites of the small with the GTPase activating center (GAC) of the large subunit. This position allows accommodation of the duplication of multilocus region 34 protein (Dom34)-dependent ribosome recycling system, which splits Lso2-containing, but not Stm1-containing, ribosomes. We propose a model in which Lso2 facilitates rapid translation reactivation by stabilizing the recycling-competent state of inactive ribosomes. PubMed: 32687489DOI: 10.1371/journal.pbio.3000780 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
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