We report crystal structures of the Thermus thermophilus ribosome at 2.3- to 2.5-Å resolution, which have enabled modeling of rRNA modifications. The structures reveal contacts of modified nucleotides with mRNA and tRNAs or protein pY, and contacts within the ribosome interior stabilizing the functional fold of rRNA. Our work provides a resource to explore the roles of rRNA modifications and yields a more comprehensive atomic model of a bacterial ribosome.
Structural insights into the role of rRNA modifications in protein synthesis and ribosome assembly
Y. Polikanov,S. Melnikov,D. Söll,T. Steitz
Published 2015 in Nature Structural &Molecular Biology
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- Publication year
2015
- Venue
Nature Structural &Molecular Biology
- Publication date
2015-03-16
- Fields of study
Biology, Medicine, Chemistry
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- External record
- Source metadata
Semantic Scholar, PubMed
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