Structure of the 30S ribosomal subunit

Wimberly, Brian T.; Brodersen, Ditlev E.; Clemons, William M.; Morgan-Warren, Robert J.; Carter, Andrew P.; Vonrhein, Clemens; Hartsch, Thomas; Ramakrishnan, V.

doi:10.1038/35030006

Cited by 2,035RNA and protein synthesis mechanismsEnzyme Structure and FunctionRNA modifications and cancer

Structure of the 30S ribosomal subunit

Wimberly, Brian T., Brodersen, Ditlev E., Clemons, William M., Morgan-Warren, Robert J., Carter, Andrew P., Vonrhein, Clemens, Hartsch, Thomas, Ramakrishnan, V.·2000·Nature

DOI 10.1038/35030006

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Abstract

Genetic information encoded in messenger RNA is translated into protein by the ribosome, which is a large nucleoprotein complex comprising two subunits, denoted 30S and 50S in bacteria. Here we report the crystal structure of the 30S subunit from Thermus thermophilus, refined to 3 A resolution. The final atomic model rationalizes over four decades of biochemical data on the ribosome, and provides a wealth of information about RNA and protein structure, protein-RNA interactions and ribosome assembly. It is also a structural basis for analysis of the functions of the 30S subunit, such as decoding, and for understanding the action of antibiotics. The structure will facilitate the interpretation in molecular terms of lower resolution structural data on several functional states of the ribosome from electron microscopy and crystallography.

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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 Wimberly et al. 2000
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From The prebiotic evolutionary advantage of transferring genetic information from RNA to DNA (2011) · cites this paper as [5]
These changes could be mediated by S12, which is in close proximity to the top of h44 and also appears to interact with Tet(O).
“These changes could be mediated by S12, which is in close proximity to the top of h44 (43, 58) and also appears to interact with Tet(O) (45).”
From Ribosomal Protection Proteins and Their Mechanism ofTetracyclineResistance (2003) · cites this paper as [58]

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Nonbridging phosphate oxygens in 16S rRNA important for 30S subunit assembly and association with the 50S ribosomal subunit
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Elongation complex of the 70S ribosome with three tRNAs and mRNA.THIS ENTRY 3I8F CONTAINS 50S RIBOSOMAL SUBUNIT. THE 30S RIBOSOMAL SUBUNIT CAN BE FOUND IN PDB ENTRY 3I8G. MOLECULE B IN THE SAME ASYMMETRIC UNIT IS DEPOSITED AS 3I8G (30S) AND 3I8F (50S).
Jenner, L. B., Yusupova, G. Z., & Yusupov, M. (2009) · Worldwide Protein Data Bank · doi:10.2210/pdb3i8f/pdb

Authors: Wimberly, B. T., Brodersen, D. E., Clemons, W. M., Morgan-Warren, R. J., Carter, A. P., Vonrhein, C., Hartsch, T., & Ramakrishnan, V.
Affiliations: MRC Laboratory of Molecular Biology (GB)
Global Phasing (United Kingdom) (GB)
University of Göttingen (DE)
Corresponding author: Ramakrishnan, V.
ORCID: Wimberly, Brian T.
Brodersen, Ditlev E.
Clemons, William M.
Carter, Andrew P.
Vonrhein, Clemens
Ramakrishnan, V.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2000-09
Volume: 407
Issue: 6802
Pages: 327-339
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/35030006
OpenAlex: W2119966574
Cited by: 2,035
References: 49
Citations by year: 2026: 20 · 2025: 24 · 2024: 26 · 2023: 37 · 2022: 36 · 2021: 46 · 2020: 47 · 2019: 45 · 2018: 38 · 2017: 52 · 2016: 41 · 2015: 56 · 2014: 71 · 2013: 59 · 2012: 85
FWCI: 52.48
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
CaltechAUTHORS (California Institute of Technology) (submittedVersion)
RePEc: Research Papers in Economics (submittedVersion)
GRO (submittedVersion)
Funders: National Institute of General Medical Sciences (F31GM019384)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
Keywords: 30S ribosomal subunit, ribosome structure, Thermus thermophilus, RNA-protein interactions, ribosome assembly, decoding, antibiotic action, crystal structure
MeSH terms: Bacterial Proteins, Models, Molecular, Nucleic Acid Conformation, Protein Conformation, Ribosomal Proteins, Ribosomes, RNA, Bacterial, RNA, Ribosomal, Thermus thermophilus, Crystallography, X-Ray, Macromolecular Substances

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Structure of the 30S ribosomal subunit

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