Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6Z6L

Cryo-EM structure of human CCDC124 bound to 80S ribosomes

This is a non-PDB format compatible entry.
Summary for 6Z6L
Entry DOI10.2210/pdb6z6l/pdb
EMDB information11098
Descriptor28S rRNA, 60S ribosomal protein L7a, 60S ribosomal protein L9, ... (85 entities in total)
Functional Keywordsribosome, hibernation
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains83
Total formula weight3905298.75
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 citationWells, 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: 32687489
DOI: 10.1371/journal.pbio.3000780
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3 Å)
Structure validation

226707

건을2024-10-30부터공개중

PDB statisticsPDBj update infoContact PDBjnumon