EMD-8418

Single-particle
10.0 Å
EMD-8418 Deposition: 04/10/2016
Map released: 23/11/2016
Last modified: 12/08/2020
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-8418

Time-resolved cryo electron microscopy map of the IF3-bound 30S subunit

EMD-8418

Single-particle
10.0 Å
EMD-8418 Deposition: 04/10/2016
Map released: 23/11/2016
Last modified: 12/08/2020
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Escherichia coli
Sample: IF3-bound 30S subunit

Deposition Authors: Fu Z, Kaledhonkar S, Borg A, Sun M, Chen B, Grassucci RA, Ehrenberg M, Frank J
Key Intermediates in Ribosome Recycling Visualized by Time-Resolved Cryoelectron Microscopy.
Fu Z , Kaledhonkar S, Borg A, Sun M , Chen B, Grassucci RA, Ehrenberg M, Frank J
(2016) Structure , 24 , 2092 - 2101
PUBMED: 27818103
DOI: doi:10.1016/j.str.2016.09.014
ISSN: 1878-4186
ASTM: STRUE6
Abstract:
Upon encountering a stop codon on mRNA, polypeptide synthesis on the ribosome is terminated by release factors, and the ribosome complex, still bound with mRNA and P-site-bound tRNA (post-termination complex, PostTC), is split into ribosomal subunits, ready for a new round of translational initiation. Separation of post-termination ribosomes into subunits, or "ribosome recycling," is promoted by the joint action of ribosome-recycling factor (RRF) and elongation factor G (EF-G) in a guanosine triphosphate (GTP) hydrolysis-dependent manner. Here we used a mixing-spraying-based method of time-resolved cryo-electron microscopy (cryo-EM) to visualize the short-lived intermediates of the recycling process. The two complexes that contain (1) both RRF and EF-G bound to the PostTC or (2) deacylated tRNA bound to the 30S subunit are of particular interest. Our observations of the native form of these complexes demonstrate the strong potential of time-resolved cryo-EM for visualizing previously unobservable transient structures.