8OM3
Small subunit of yeast mitochondrial ribosome in complex with IF3/Aim23.
This is a non-PDB format compatible entry.
Summary for 8OM3
| Entry DOI | 10.2210/pdb8om3/pdb |
| EMDB information | 16967 17094 17095 17096 17097 |
| Descriptor | 37S ribosomal protein MRP51, mitochondrial, 37S ribosomal protein S10, mitochondrial, 37S ribosomal protein S18, mitochondrial, ... (40 entities in total) |
| Functional Keywords | mitochondria, initiation factor 3, pre-initiation complex, ribosome |
| Biological source | Saccharomyces cerevisiae (baker's yeast) More |
| Total number of polymer chains | 35 |
| Total formula weight | 1513707.17 |
| Authors | Itoh, Y.,Chicherin, I.,Kamenski, P.,Amunts, A. (deposition date: 2023-03-31, release date: 2024-01-10, Last modification date: 2024-11-13) |
| Primary citation | Ast, T.,Itoh, Y.,Sadre, S.,McCoy, J.G.,Namkoong, G.,Wengrod, J.C.,Chicherin, I.,Joshi, P.R.,Kamenski, P.,Suess, D.L.M.,Amunts, A.,Mootha, V.K. METTL17 is an Fe-S cluster checkpoint for mitochondrial translation. Mol.Cell, 84:359-, 2024 Cited by PubMed Abstract: Friedreich's ataxia (FA) is a debilitating, multisystemic disease caused by the depletion of frataxin (FXN), a mitochondrial iron-sulfur (Fe-S) cluster biogenesis factor. To understand the cellular pathogenesis of FA, we performed quantitative proteomics in FXN-deficient human cells. Nearly every annotated Fe-S cluster-containing protein was depleted, indicating that as a rule, cluster binding confers stability to Fe-S proteins. We also observed depletion of a small mitoribosomal assembly factor METTL17 and evidence of impaired mitochondrial translation. Using comparative sequence analysis, mutagenesis, biochemistry, and cryoelectron microscopy, we show that METTL17 binds to the mitoribosomal small subunit during late assembly and harbors a previously unrecognized [FeS] cluster required for its stability. METTL17 overexpression rescued the mitochondrial translation and bioenergetic defects, but not the cellular growth, of FXN-depleted cells. These findings suggest that METTL17 acts as an Fe-S cluster checkpoint, promoting translation of Fe-S cluster-rich oxidative phosphorylation (OXPHOS) proteins only when Fe-S cofactors are replete. PubMed: 38199006DOI: 10.1016/j.molcel.2023.12.016 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.87 Å) |
Structure validation
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