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- Publisher
- Springer Journals
- Copyright
- Copyright © 2000 by Nature America Inc.
- Subject
- Life Sciences; Life Sciences, general; Biochemistry, general; Protein Structure; Membrane Biology; Biological Microscopy
- ISSN
- 1545-9993
- eISSN
- 1545-9985
- DOI
- 10.1038/74028
- Publisher site
- See Article on Publisher Site
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 Å 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.
Journal
Nature Structural & Molecular Biology – Springer Journals
Published: Apr 1, 2000