Crystal structure of the ribosome at 5.5 Å resolution
Abstract
We describe the crystal structure of the complete Thermus thermophilus 70 S ribosome containing bound messenger RNA and transfer RNAs (tRNAs) at 5.5 angstrom resolution. All of the 16 S , 23 S , and 5 S ribosomal RNA (rRNA) chains, the A-, P-, and E-site tRNAs, and most of the ribosomal proteins can be fitted to the electron density map. The core of the interface between the 30 S small subunit and the 50 S large subunit, where the tRNA substrates are bound, is dominated by RNA, with proteins located mainly at the periphery, consistent with ribosomal function being based on rRNA. In each of the three tRNA binding sites, the ribosome contacts all of the major elements of tRNA, providing an explanation for the conservation of tRNA structure. The tRNAs are closely juxtaposed with the intersubunit bridges, in a way that suggests coupling of the 20 to 50 angstrom movements associated with tRNA translocation with intersubunit movement.
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The RNA World theory's plausibility is bolstered by experimental findings including centrality of RNA nucleotides in metabolism, nature of the ribosome, and abiotic synthesis of RNA nucleosides.
“The plausibility of this theory is bolstered by several experimental findings, including the centrality of RNA nucleotides in metabolism, the nature of the ribosome (a ribozyme) (Ban et al. 2000; Wimberly et al. 2000; Yusupov et al. 2001), and the abiotic synthesis of RNA nucleosides (Powner et al. 2009).”
From The paradox of dual roles in the RNA world: resolving the conflict between stable folding and templating ability (2013) · cites this paper as Yusupov et al. 2001
The catalytic core of the ribosome comprises RNA.
“The finding that the catalytic core of the ribosome comprises RNA lent considerable credence to the RNA world theory (4–6).”
From The prebiotic evolutionary advantage of transferring genetic information from RNA to DNA (2011) · cites this paper as [6]
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- Authors
- Yusupov, M. M., Yusupova, G. Z., Baucom, A., Lieberman, K., Earnest, T. N., Cate, J. H. D., & Noller, H. F.
- Affiliations
- University of California, Santa Cruz (US)
- Lawrence Berkeley National Laboratory (US)
- Whitehead Institute for Biomedical Research (US)
- Corresponding author
- Yusupov, Marat M.
- Yusupova, Gulnara Zh.
- Cate, J. H. D.
- Noller, Harry F.
- Venue
- Science
- Published
- 2001-05-04
- Volume
- 292
- Issue
- 5518
- Pages
- 883-896
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2093471887
- Cited by
- 1,944
- References
- 74
- Citations by year
- 2026: 18 · 2025: 26 · 2024: 34 · 2023: 26 · 2022: 40 · 2021: 36 · 2020: 45 · 2019: 31 · 2018: 37 · 2017: 48 · 2016: 47 · 2015: 57 · 2014: 67 · 2013: 69 · 2012: 83
- FWCI
- 51.20
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- HAL (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- ribosome, Thermus thermophilus, 70S ribosome, ribosomal RNA, tRNA binding sites, tRNA translocation, ribosomal proteins, mRNA
- MeSH terms
- Anticodon, Bacterial Proteins, Base Sequence, Binding Sites, Models, Molecular, Molecular Sequence Data, Nucleic Acid Conformation, Protein Conformation, Ribosomal Proteins, Ribosomes, RNA, Bacterial, RNA, Messenger, RNA, Ribosomal, RNA, Transfer, RNA, Transfer, Amino Acid-Specific, Protein Biosynthesis, Thermus thermophilus, Crystallography, X-Ray
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