Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural mechanism of GTPase-powered ribosome-tRNA movement.
Journal, issue, pages	Nat Commun, Vol. 12, Issue 1, Page 5933, Year 2021
Publish date	Oct 11, 2021
Authors	Valentyn Petrychenko / Bee-Zen Peng / Ana C de A P Schwarzer / Frank Peske / Marina V Rodnina / Niels Fischer /
PubMed Abstract	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.
External links	Nat Commun / PubMed:34635670 / PubMed Central
Methods	EM (single particle)
Resolution	2.35 - 9.5 Å
Structure data	13458 7pjs EMDB-13458, PDB-7pjs: Structure of the 70S ribosome with tRNAs in the classical pre-translocation state and apramycin (C) Method: EM (single particle) / Resolution: 2.35 Å 13459 7pjt EMDB-13459, PDB-7pjt: Structure of the 70S ribosome with tRNAs in hybrid state 1 (H1) Method: EM (single particle) / Resolution: 6.0 Å 13460 7pju EMDB-13460, PDB-7pju: Structure of the 70S ribosome with tRNAs in hybrid state 2 (H2) Method: EM (single particle) / Resolution: 9.5 Å 13461 7pjv EMDB-13461, PDB-7pjv: Structure of the 70S-EF-G-GDP-Pi ribosome complex with tRNAs in hybrid state 1 (H1-EF-G-GDP-Pi) Method: EM (single particle) / Resolution: 3.1 Å 13462 7pjw EMDB-13462, PDB-7pjw: Structure of the 70S-EF-G-GDP-Pi ribosome complex with tRNAs in hybrid state 2 (H2-EF-G-GDP-Pi) Method: EM (single particle) / Resolution: 4.0 Å 13463 7pjx EMDB-13463, PDB-7pjx: Structure of the 70S-EF-G-GDP ribosome complex with tRNAs in hybrid state 1 (H1-EF-G-GDP) Method: EM (single particle) / Resolution: 6.5 Å 13464 7pjy EMDB-13464, PDB-7pjy: Structure of the 70S-EF-G-GDP ribosome complex with tRNAs in chimeric state 1 (CHI1-EF-G-GDP) Method: EM (single particle) / Resolution: 3.1 Å 13465 7pjz EMDB-13465, PDB-7pjz: Structure of the 70S-EF-G-GDP ribosome complex with tRNAs in chimeric state 2 (CHI2-EF-G-GDP) Method: EM (single particle) / Resolution: 6.0 Å
Chemicals	ChemComp-MG: Unknown entry ChemComp-ZN: Unknown entry ChemComp-NA: Unknown entry ChemComp-AM2: APRAMYCIN / antibioticYM / Apramycin ChemComp-HOH: WATER / Water ChemComp-GDP: GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying moleculeYM / Guanosine diphosphate ChemComp-PO4: PHOSPHATE ION / Phosphate
Source	escherichia coli (E. coli) escherichia coli (strain k12) (bacteria)
Keywords	RIBOSOME / EF-G / robosome / 70S / apramycin / translocation