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6YW5

The structure of the small subunit of the mitoribosome from Neurospora crassa

This is a non-PDB format compatible entry.
Summary for 6YW5
Entry DOI10.2210/pdb6yw5/pdb
EMDB information10958
DescriptoruS2m, 37S ribosomal protein S10, mitochondrial, Mitochondrial ribosomal protein subunit S18, ... (39 entities in total)
Functional Keywordsneurospora crassa, translating mitoribosomes, trna, mrna, ml108, translation
Biological sourceNeurospora crassa OR74A
More
Total number of polymer chains38
Total formula weight1760317.01
Authors
Amunts, A.,Itoh, Y.,Naschberger, A. (deposition date: 2020-04-29, release date: 2020-11-11, Last modification date: 2024-11-06)
Primary citationItoh, 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: 33056988
DOI: 10.1038/s41467-020-18830-w
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.85 Å)
Structure validation

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