6YWV
The structure of the Atp25 bound assembly intermediate of the mitoribosome from Neurospora crassa
This is a non-PDB format compatible entry.
Summary for 6YWV
Entry DOI | 10.2210/pdb6ywv/pdb |
EMDB information | 10977 |
Descriptor | 23 S rRNA, 50S ribosomal protein L14, 50S ribosomal subunit protein L15, ... (48 entities in total) |
Functional Keywords | neurospora crassa, translating mitoribosomes, trna, mrna, ml108, translation |
Biological source | Neurospora crassa OR74A More |
Total number of polymer chains | 43 |
Total formula weight | 2356131.02 |
Authors | Amunts, A.,Itoh, Y.,Naschberger, A. (deposition date: 2020-04-30, release date: 2020-11-11, Last modification date: 2024-05-22) |
Primary citation | Itoh, Y.,Naschberger, A.,Mortezaei, N.,Herrmann, J.M.,Amunts, A. Analysis of translating mitoribosome reveals functional characteristics of translation in mitochondria of fungi. Nat Commun, 11:5187-5187, 2020 Cited by PubMed Abstract: Mitoribosomes are specialized protein synthesis machineries in mitochondria. However, how mRNA binds to its dedicated channel, and tRNA moves as the mitoribosomal subunit rotate with respect to each other is not understood. We report models of the translating fungal mitoribosome with mRNA, tRNA and nascent polypeptide, as well as an assembly intermediate. Nicotinamide adenine dinucleotide (NAD) is found in the central protuberance of the large subunit, and the ATPase inhibitory factor 1 (IF) in the small subunit. The models of the active mitoribosome explain how mRNA binds through a dedicated protein platform on the small subunit, tRNA is translocated with the help of the protein mL108, bridging it with L1 stalk on the large subunit, and nascent polypeptide paths through a newly shaped exit tunnel involving a series of structural rearrangements. An assembly intermediate is modeled with the maturation factor Atp25, providing insight into the biogenesis of the mitoribosomal large subunit and translation regulation. PubMed: 33056988DOI: 10.1038/s41467-020-18830-w PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.03 Å) |
Structure validation
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