English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
  Local TagsRelease HistoryDetailsSummary

Released
Journal Article

The pathway to GTPase activation of elongation factor SelB on the ribosome.

MPS-Authors
/persons/resource/persons135076

Maracci,  C.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15360

Konevega,  A. L.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15155

Grubmüller,  H.
Department of Theoretical and Computational Biophysics, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15723

Rodnina,  M. V.
Department of Physical Biochemistry, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15857

Stark,  H.
Department of Structural Dynamics, MPI for Biophysical Chemistry, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)

2357895.pdf
(Publisher version), 26MB

Supplementary Material (public)
There is no public supplementary material available
Citation

Fischer, N., Neumann, P., Bock, l. V., Maracci, C., Wang, Z., Paleskava, A., et al. (2016). The pathway to GTPase activation of elongation factor SelB on the ribosome. Nature, 540(7631), 80-85. doi:10.1038/nature20560.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002B-B6A1-F
Abstract
In all domains of life, selenocysteine (Sec) is delivered to the ribosome by selenocysteine-specific tRNA (tRNASec) with the help of a specialized translation factor, SelB in bacteria. Sec-tRNASec recodes a UGA stop codon next to a downstream mRNA stem-loop. Here we present the structures of six intermediates on the pathway of UGA recoding in Escherichia coli by single-particle cryo-electron microscopy. The structures explain the specificity of Sec-tRNASec binding by SelB and show large-scale rearrangements of Sec-tRNASec. Upon initial binding of SelB-Sec-tRNASec to the ribosome and codon reading, the 30S subunit adopts an open conformation with Sec-tRNASec covering the sarcin-ricin loop (SRL) on the 50S subunit. Subsequent codon recognition results in a local closure of the decoding site, which moves Sec-tRNASec away from the SRL and triggers a global closure of the 30S subunit shoulder domain. As a consequence, SelB docks on the SRL, activating the GTPase of SelB. These results reveal how codon recognition triggers GTPase activation in translational GTPases.