6NU3
Structural insights into unique features of the human mitochondrial ribosome recycling
This is a non-PDB format compatible entry.
Summary for 6NU3
| Entry DOI | 10.2210/pdb6nu3/pdb |
| EMDB information | 0515 |
| Descriptor | 16S rRNA, 39S ribosomal protein L14, mitochondrial, 39S ribosomal protein L15, mitochondrial, ... (87 entities in total) |
| Functional Keywords | mitochondrial ribosome recycling factor, mtrrf, 55s, ribosome |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 85 |
| Total formula weight | 2799251.39 |
| Authors | Sharma, M.R.,Koripella, R.K.,Agrawal, R.K. (deposition date: 2019-01-30, release date: 2019-04-17, Last modification date: 2024-10-23) |
| Primary citation | Koripella, R.K.,Sharma, M.R.,Risteff, P.,Keshavan, P.,Agrawal, R.K. Structural insights into unique features of the human mitochondrial ribosome recycling. Proc.Natl.Acad.Sci.USA, 116:8283-8288, 2019 Cited by PubMed Abstract: Mammalian mitochondrial ribosomes (mitoribosomes) are responsible for synthesizing proteins that are essential for oxidative phosphorylation (ATP generation). Despite their common ancestry with bacteria, the composition and structure of the human mitoribosome and its translational factors are significantly different from those of their bacterial counterparts. The mammalian mitoribosome recycling factor (RRF) carries a mito-specific N terminus extension (NTE), which is necessary for the function of RRF Here we present a 3.9-Å resolution cryo-electron microscopic (cryo-EM) structure of the human 55S mitoribosome-RRF complex, which reveals α-helix and loop structures for the NTE that makes multiple mito-specific interactions with functionally critical regions of the mitoribosome. These include ribosomal RNA segments that constitute the peptidyl transferase center (PTC) and those that connect PTC with the GTPase-associated center and with mitoribosomal proteins L16 and L27. Our structure reveals the presence of a tRNA in the pe/E position and a rotation of the small mitoribosomal subunit on RRF binding. In addition, we observe an interaction between the pe/E tRNA and a mito-specific protein, mL64. These findings help understand the unique features of mitoribosome recycling. PubMed: 30962385DOI: 10.1073/pnas.1815675116 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.4 Å) |
Structure validation
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