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-Structure paper
タイトル | Structural mechanism of GTPase-powered ribosome-tRNA movement. |
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ジャーナル・号・ページ | Nat Commun, Vol. 12, Issue 1, Page 5933, Year 2021 |
掲載日 | 2021年10月11日 |
著者 | Valentyn Petrychenko / Bee-Zen Peng / Ana C de A P Schwarzer / Frank Peske / Marina V Rodnina / Niels Fischer / |
PubMed 要旨 | GTPases are regulators of cell signaling acting as molecular switches. The translational GTPase EF-G stands out, as it uses GTP hydrolysis to generate force and promote the movement of the ribosome ...GTPases are regulators of cell signaling acting as molecular switches. The translational GTPase EF-G stands out, as it uses GTP hydrolysis to generate force and promote the movement of the ribosome along the mRNA. The key unresolved question is how GTP hydrolysis drives molecular movement. Here, we visualize the GTPase-powered step of ongoing translocation by time-resolved cryo-EM. EF-G in the active GDP-Pi form stabilizes the rotated conformation of ribosomal subunits and induces twisting of the sarcin-ricin loop of the 23 S rRNA. Refolding of the GTPase switch regions upon Pi release initiates a large-scale rigid-body rotation of EF-G pivoting around the sarcin-ricin loop that facilitates back rotation of the ribosomal subunits and forward swiveling of the head domain of the small subunit, ultimately driving tRNA forward movement. The findings demonstrate how a GTPase orchestrates spontaneous thermal fluctuations of a large RNA-protein complex into force-generating molecular movement. |
リンク | Nat Commun / PubMed:34635670 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.35 - 9.5 Å |
構造データ | EMDB-13458, PDB-7pjs: EMDB-13459, PDB-7pjt: EMDB-13460, PDB-7pju: EMDB-13461, PDB-7pjv: EMDB-13462, PDB-7pjw: EMDB-13463, PDB-7pjx: EMDB-13464, PDB-7pjy: EMDB-13465, PDB-7pjz: |
化合物 | ChemComp-MG: ChemComp-ZN: ChemComp-NA: ChemComp-AM2: ChemComp-HOH: ChemComp-GDP: ChemComp-PO4: |
由来 |
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キーワード | RIBOSOME / EF-G / robosome / 70S / apramycin / translocation |