1MMS
Crystal structure of the ribosomal PROTEIN L11-RNA complex
1MMS の概要
| エントリーDOI | 10.2210/pdb1mms/pdb |
| 分子名称 | 23S RIBOSOMAL RNA, PROTEIN (RIBOSOMAL PROTEIN L11), CADMIUM ION, ... (6 entities in total) |
| 機能のキーワード | rna-protein complex, rna, ribosome, translocation, thiostrepton |
| 由来する生物種 | Thermotoga maritima 詳細 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 70433.82 |
| 構造登録者 | Wimberly, B.T.,Guymon, R.,Mccutcheon, J.P.,White, S.W.,Ramakrishnan, V. (登録日: 1999-04-14, 公開日: 2000-04-17, 最終更新日: 2023-12-27) |
| 主引用文献 | Wimberly, B.T.,Guymon, R.,McCutcheon, J.P.,White, S.W.,Ramakrishnan, V. A detailed view of a ribosomal active site: the structure of the L11-RNA complex. Cell(Cambridge,Mass.), 97:491-502, 1999 Cited by PubMed Abstract: We report the crystal structure of a 58 nucleotide fragment of 23S ribosomal RNA bound to ribosomal protein L11. This highly conserved ribonucleoprotein domain is the target for the thiostrepton family of antibiotics that disrupt elongation factor function. The highly compact RNA has both familiar and novel structural motifs. While the C-terminal domain of L11 binds RNA tightly, the N-terminal domain makes only limited contacts with RNA and is proposed to function as a switch that reversibly associates with an adjacent region of RNA. The sites of mutations conferring resistance to thiostrepton and micrococcin line a narrow cleft between the RNA and the N-terminal domain. These antibiotics are proposed to bind in this cleft, locking the putative switch and interfering with the function of elongation factors. PubMed: 10338213DOI: 10.1016/S0092-8674(00)80759-X 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.57 Å) |
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