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1X18

Contact sites of ERA GTPase on the THERMUS THERMOPHILUS 30S SUBUNIT

1X18 の概要
エントリーDOI10.2210/pdb1x18/pdb
関連するPDBエントリー1EGA 1FJF 1WF3 1X1L
分子名称5'-R(P*CP*GP*AP*UP*GP*GP*CP*GP*AP*AP*G)-3', RNA (31-MER), 5'-R(P*UP*UP*CP*CP*CP*GP*GP*GP*CP*CP*UP*GP*GP*GP*GP*CP*CP*CP*GP*C)-3', ... (9 entities in total)
機能のキーワードcontact sites of era protein on the 30s ribosomal subunit, structural protein-rna complex, structural protein/rna
由来する生物種Thermus thermophilus
詳細
タンパク質・核酸の鎖数9
化学式量合計126115.64
構造登録者
Sharma, M.R.,Barat, C.,Agrawal, R.K. (登録日: 2005-04-02, 公開日: 2005-05-17, 最終更新日: 2024-03-13)
主引用文献Sharma, M.R.,Barat, C.,Wilson, D.N.,Booth, T.M.,Kawazoe, M.,Hori-Takemoto, C.,Shirouzu, M.,Yokoyama, S.,Fucini, P.,Agrawal, R.K.
Interaction of Era with the 30S Ribosomal Subunit Implications for 30S Subunit Assembly
Mol.Cell, 18:319-329, 2005
Cited by
PubMed Abstract: 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.
PubMed: 15866174
DOI: 10.1016/j.molcel.2005.03.028
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (13.5 Å)
構造検証レポート
Validation report summary of 1x18
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-20に公開中

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