Summary information and primary citation

PDB-id
3j5s; SNAP-derived features in text and JSON formats; DNAproDB
Class
ribosome-translation
Method
cryo-EM (7.5 Å)
Summary
Etta binds to ribosome exit site and regulates translation by restricting ribosome and trna dynamics
Reference
Chen B, Boel G, Hashem Y, Ning W, Fei J, Wang C, Gonzalez RL, Hunt JF, Frank J (2014): "EttA regulates translation by binding the ribosomal E site and restricting ribosome-tRNA dynamics." Nat.Struct.Mol.Biol., 21, 152-159. doi: 10.1038/nsmb.2741.
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.

Cartoon-block schematics in six views (download the tarball)

PyMOL session file Download PDB file View in 3Dmol.js