4V85
Crystal Structure of Release Factor RF3 Trapped in the GTP State on a Rotated Conformation of the Ribosome.
これはPDB形式変換不可エントリーです。
4V85 の概要
エントリーDOI | 10.2210/pdb4v85/pdb |
関連するBIRD辞書のPRD_ID | PRD_000226 |
分子名称 | 16S rRNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (59 entities in total) |
機能のキーワード | typeii release factor binding with ribosome, ribosome-antibiotic complex, ribosome/antibiotic |
由来する生物種 | Escherichia coli 詳細 |
タンパク質・核酸の鎖数 | 59 |
化学式量合計 | 2274150.43 |
構造登録者 | Zhou, J.,Lancaster, L.,Trakhanov, S.,Noller, H.F. (登録日: 2011-06-13, 公開日: 2014-07-09, 最終更新日: 2019-07-17) |
主引用文献 | Zhou, J.,Lancaster, L.,Trakhanov, S.,Noller, H.F. Crystal structure of release factor RF3 trapped in the GTP state on a rotated conformation of the ribosome. Rna, 18:230-240, 2012 Cited by PubMed Abstract: The class II release factor RF3 is a GTPase related to elongation factor EF-G, which catalyzes release of class I release factors RF1 and RF2 from the ribosome after termination of protein synthesis. The 3.3 Å crystal structure of the RF3·GDPNP·ribosome complex provides a high-resolution description of interactions and structural rearrangements that occur when binding of this translational GTPase induces large-scale rotational movements in the ribosome. RF3 induces a 7° rotation of the body and 14° rotation of the head of the 30S ribosomal subunit, and itself undergoes inter- and intradomain conformational rearrangements. We suggest that ordering of critical elements of switch loop I and the P loop, which help to form the GTPase catalytic site, are caused by interactions between the G domain of RF3 and the sarcin-ricin loop of 23S rRNA. The rotational movements in the ribosome induced by RF3, and its distinctly different binding orientation to the sarcin-ricin loop of 23S rRNA, raise interesting implications for the mechanism of action of EF-G in translocation. PubMed: 22187675DOI: 10.1261/rna.031187.111 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.2 Å) |
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