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-Structure paper
タイトル | Interaction of Era with the 30S ribosomal subunit implications for 30S subunit assembly. |
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ジャーナル・号・ページ | Mol Cell, Vol. 18, Issue 3, Page 319-329, Year 2005 |
掲載日 | 2005年4月29日 |
著者 | Manjuli R Sharma / Chandana Barat / Daniel N Wilson / Timothy M Booth / Masahito Kawazoe / Chie Hori-Takemoto / Mikako Shirouzu / Shigeyuki Yokoyama / Paola Fucini / Rajendra K Agrawal / |
PubMed 要旨 | Era (E. coliRas-like protein) is a highly conserved and essential GTPase in bacteria. It binds to the 16S ribosomal RNA (rRNA) of the small (30S) ribosomal subunit, and its depletion leads to ...Era (E. coliRas-like protein) is a highly conserved and essential GTPase in bacteria. It binds to the 16S ribosomal RNA (rRNA) of the small (30S) ribosomal subunit, and its depletion leads to accumulation of an unprocessed precursor of the 16S rRNA. We have obtained a three-dimensional cryo-electron microscopic map of the Thermus thermophilus 30S-Era complex. Era binds in the cleft between the head and platform of the 30S subunit and locks the subunit in a conformation that is not favorable for association with the large (50S) ribosomal subunit. The RNA binding KH motif present within the C-terminal domain of Era interacts with the conserved nucleotides in the 3' region of the 16S rRNA. Furthermore, Era makes contact with several assembly elements of the 30S subunit. These observations suggest a direct involvement of Era in the assembly and maturation of the 30S subunit. |
リンク | Mol Cell / PubMed:15866174 |
手法 | EM (単粒子) |
解像度 | 13.5 Å |
構造データ | PDB-1x18: PDB-1x1l: |
由来 |
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キーワード | STRUCTURAL PROTEIN/RNA / Contact sites of Era protein on the 30S ribosomal subunit / STRUCTURAL PROTEIN-RNA COMPLEX / Interaction of Era protein with the 3'minor domain of 16S rRNA |