Crystal structure of the S15-rRNA complex.
Abstract
In bacterial ribosomes, the small (30S) ribosomal subunit is composed of 16S rRNA and 21 distinct proteins. Ribosomal protein S15 is of particular interest because it binds primarily to 16S rRNA and is required for assembly of the small subunit and for intersubunit association, thus representing a key element in the assembly of a whole ribosome. Here we report the 2.8 ¿ resolution crystal structure of the highly conserved S15-rRNA complex. Protein S15 interacts in the minor groove with a G-U/G-C motif and a three-way junction. The latter is constrained by a conserved base triple and stacking interactions, and locked into place by magnesium ions and protein side chains, mainly through interactions with the unique three-dimensional geometry of the backbone. The present structure gives insights into the dual role of S15 in ribosome assembly and translational regulation.
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The changes added by human players tend to agree with the 16S structural model, especially in regions linked to important functional sites, such as S8 and S15 binding sites, and a region that undergoes conformational readjustment during 30S assembly.
“In Fig. 4, we show that the changes added by human players tend to agree with the 16S structural model, especially in regions linked to important functional sites, such as S8 and S15 binding sites, and a region that undergoes conformational readjustment during 30S assembly44–49.”
From Improving microbial phylogeny with citizen science within a mass-market video game (2025) · cites this paper as [47]
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- Authors
- Dumas, P., Никулин, А. Д., Serganov, A., Ennifar, E., Tishchenko, S., Nevskaya, N. A., Shepard, W., Portier, C., Garber, M., Ehresmann, B., Ehresmann, C., & Nikonov, S. V.
- Affiliations
- Centre National de la Recherche Scientifique (FR)
- Institute of Protein Research (RU)
- Université Paris-Sud (FR)
- Institut de Biologie Physico-Chimique (FR)
- Corresponding author
- Philippe Dumas
- Venue
- Nature Structural Biology
- Published
- 2000-04-01
- Volume
- 7
- Issue
- 4
- Pages
- 273-277
- ISSN
- 1072-8368 (ISSN-L)
- OpenAlex
- W2153875623
- Cited by
- 80
- References
- 0
- Citations by year
- 2026: 1 · 2025: 1 · 2024: 1 · 2022: 1 · 2021: 4 · 2020: 1 · 2018: 2 · 2016: 3 · 2015: 1 · 2013: 3 · 2012: 4
- FWCI
- 3.74
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature Structural Biology (publishedVersion)
- PubMed (publishedVersion)
- 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
- ribosomal protein S15, 16S rRNA, 30S ribosomal subunit, ribosome assembly, three-way junction, base triple, magnesium ions, minor groove, translational regulation, bacterial ribosome
- MeSH terms
- Amino Acid Sequence, Base Sequence, Binding Sites, Magnesium, Models, Molecular, Molecular Sequence Data, Nucleic Acid Conformation, Protein Conformation, Ribosomal Proteins, RNA, Bacterial, RNA, Ribosomal, 16S, Structure-Activity Relationship, Thermus thermophilus, Conserved Sequence, Crystallography, X-Ray, Base Pairing
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