7SSN
Pre translocation 70S ribosome with A/P* and P/E tRNA (Structure II-B)
This is a non-PDB format compatible entry.
Summary for 7SSN
Entry DOI | 10.2210/pdb7ssn/pdb |
EMDB information | 25405 25407 25409 25410 25411 25415 25418 |
Descriptor | 16S rRNA, 50S ribosomal protein L11, 50S ribosomal protein L13, ... (54 entities in total) |
Functional Keywords | ribosome, hybrid, translocation |
Biological source | Escherichia coli K-12 More |
Total number of polymer chains | 54 |
Total formula weight | 2165159.93 |
Authors | |
Primary citation | Carbone, C.E.,Loveland, A.B.,Gamper Jr., H.B.,Hou, Y.M.,Demo, G.,Korostelev, A.A. Time-resolved cryo-EM visualizes ribosomal translocation with EF-G and GTP. Nat Commun, 12:7236-7236, 2021 Cited by PubMed Abstract: During translation, a conserved GTPase elongation factor-EF-G in bacteria or eEF2 in eukaryotes-translocates tRNA and mRNA through the ribosome. EF-G has been proposed to act as a flexible motor that propels tRNA and mRNA movement, as a rigid pawl that biases unidirectional translocation resulting from ribosome rearrangements, or by various combinations of motor- and pawl-like mechanisms. Using time-resolved cryo-EM, we visualized GTP-catalyzed translocation without inhibitors, capturing elusive structures of ribosome•EF-G intermediates at near-atomic resolution. Prior to translocation, EF-G binds near peptidyl-tRNA, while the rotated 30S subunit stabilizes the EF-G GTPase center. Reverse 30S rotation releases Pi and translocates peptidyl-tRNA and EF-G by ~20 Å. An additional 4-Å translocation initiates EF-G dissociation from a transient ribosome state with highly swiveled 30S head. The structures visualize how nearly rigid EF-G rectifies inherent and spontaneous ribosomal dynamics into tRNA-mRNA translocation, whereas GTP hydrolysis and Pi release drive EF-G dissociation. PubMed: 34903725DOI: 10.1038/s41467-021-27415-0 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
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