3J5S

EttA binds to ribosome exit site and regulates translation by restricting ribosome and tRNA dynamics

Summary for 3J5S

• Entry DOI: 10.2210/pdb3j5s/pdb
• EMDB information: 5784
• Descriptor: 16S ribosomal RNA, 23S ribosomal RNA, P-site tRNA FMet, ... (8 entities in total)
• Functional Keywords: protein translation regulation, abc-f protein family, single-molecule fret, yjjk, ribosome-translation complex, ribosome/translation
• Biological source: Escherichia coli; More
• Total number of polymer chains: 8
• Total formula weight: 304683.94

Authors

Hashem, Y. (deposition date: 2013-11-15, release date: 2014-01-08, Last modification date: 2024-02-21)

Primary citation

Chen, B.,Boel, G.,Hashem, Y.,Ning, W.,Fei, J.,Wang, C.,Gonzalez, R.L.,Hunt, J.F.,Frank, J.
EttA regulates translation by binding the ribosomal E site and restricting ribosome-tRNA dynamics.
Nat.Struct.Mol.Biol., 21:152-159, 2014

PubMed Abstract: Cells express many ribosome-interacting factors whose functions and molecular mechanisms remain unknown. Here, we elucidate the mechanism of a newly characterized regulatory translation factor, energy-dependent translational throttle A (EttA), which is an Escherichia coli representative of the ATP-binding cassette F (ABC-F) protein family. Using cryo-EM, we demonstrate that the ATP-bound form of EttA binds to the ribosomal tRNA-exit site, where it forms bridging interactions between the ribosomal L1 stalk and the tRNA bound in the peptidyl-tRNA-binding site. Using single-molecule fluorescence resonance energy transfer, we show that the ATP-bound form of EttA restricts ribosome and tRNA dynamics required for protein synthesis. This work represents the first example, to our knowledge, in which the detailed molecular mechanism of any ABC-F family protein has been determined and establishes a framework for elucidating the mechanisms of other regulatory translation factors.

PubMed: 24389465
DOI: 10.1038/nsmb.2741

Experimental method

ELECTRON MICROSCOPY (7.5 Å)