1DK1
DETAILED VIEW OF A KEY ELEMENT OF THE RIBOSOME ASSEMBLY: CRYSTAL STRUCTURE OF THE S15-RRNA COMPLEX
1DK1 の概要
| エントリーDOI | 10.2210/pdb1dk1/pdb |
| 分子名称 | RRNA FRAGMENT, 30S RIBOSOMAL PROTEIN S15, MAGNESIUM ION, ... (6 entities in total) |
| 機能のキーワード | ribosome, s15, protein, rna |
| 由来する生物種 | Thermus thermophilus 詳細 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 29267.49 |
| 構造登録者 | Nikulin, A.,Serganov, A.,Ennifar, E.,Tischenko, S.,Nevskaya, N. (登録日: 1999-12-06, 公開日: 2000-04-02, 最終更新日: 2024-10-30) |
| 主引用文献 | Nikulin, A.,Serganov, A.,Ennifar, E.,Tishchenko, S.,Nevskaya, N.,Shepard, W.,Portier, C.,Garber, M.,Ehresmann, B.,Ehresmann, C.,Nikonov, S.,Dumas, P. Crystal structure of the S15-rRNA complex. Nat.Struct.Biol., 7:273-277, 2000 Cited by PubMed 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. PubMed: 10742169DOI: 10.1038/74028 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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