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6S47

Saccharomyces cerevisiae 80S ribosome bound with ABCF protein New1

This is a non-PDB format compatible entry.
Summary for 6S47
Entry DOI10.2210/pdb6s47/pdb
EMDB information10098
Descriptor28S ribosomal RNA, 60S ribosomal protein L8-A, 60S ribosomal protein L9-A, ... (80 entities in total)
Functional Keywordsnew1, abcf, ribosomal protein, recycling, termination, translation
Biological sourceSaccharomyces cerevisiae (Baker's yeast)
More
Total number of polymer chains79
Total formula weight3095314.83
Authors
Kasari, V.,Pochopien, A.A.,Margus, T.,Murina, V.,Turnbull, K.,Zhou, Y.,Nissan, T.,Graf, M.,Novacek, J.,Atkinson, G.C.,Johansson, M.J.O.,Wilson, D.N.,Hauryliuk, V. (deposition date: 2019-06-26, release date: 2019-07-24, Last modification date: 2025-04-09)
Primary citationKasari, V.,Pochopien, A.A.,Margus, T.,Murina, V.,Turnbull, K.,Zhou, Y.,Nissan, T.,Graf, M.,Novacek, J.,Atkinson, G.C.,Johansson, M.J.O.,Wilson, D.N.,Hauryliuk, V.
A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling.
Nucleic Acids Res., 47:8807-8820, 2019
Cited by
PubMed Abstract: Translation is controlled by numerous accessory proteins and translation factors. In the yeast Saccharomyces cerevisiae, translation elongation requires an essential elongation factor, the ABCF ATPase eEF3. A closely related protein, New1, is encoded by a non-essential gene with cold sensitivity and ribosome assembly defect knock-out phenotypes. Since the exact molecular function of New1 is unknown, it is unclear if the ribosome assembly defect is direct, i.e. New1 is a bona fide assembly factor, or indirect, for instance due to a defect in protein synthesis. To investigate this, we employed yeast genetics, cryo-electron microscopy (cryo-EM) and ribosome profiling (Ribo-Seq) to interrogate the molecular function of New1. Overexpression of New1 rescues the inviability of a yeast strain lacking the otherwise strictly essential translation factor eEF3. The structure of the ATPase-deficient (EQ2) New1 mutant locked on the 80S ribosome reveals that New1 binds analogously to the ribosome as eEF3. Finally, Ribo-Seq analysis revealed that loss of New1 leads to ribosome queuing upstream of 3'-terminal lysine and arginine codons, including those genes encoding proteins of the cytoplasmic translational machinery. Our results suggest that New1 is a translation factor that fine-tunes the efficiency of translation termination or ribosome recycling.
PubMed: 31299085
DOI: 10.1093/nar/gkz600
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.28 Å)
Structure validation

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