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5LZA

Structure of the 70S ribosome with SECIS-mRNA and P-site tRNA (Initial complex, IC)

This is a non-PDB format compatible entry.
Summary for 5LZA
Entry DOI10.2210/pdb5lza/pdb
EMDB information4121
Descriptor16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (56 entities in total)
Functional Keywordstranslation, decoding, recoding, selenocysteine, ribosome
Biological sourceEscherichia coli
More
Total number of polymer chains55
Total formula weight2167401.69
Authors
Fischer, N.,Neumann, P.,Bock, L.V.,Maracci, C.,Wang, Z.,Paleskava, A.,Konevega, A.L.,Schroeder, G.F.,Grubmueller, H.,Ficner, R.,Rodnina, M.V.,Stark, H. (deposition date: 2016-09-29, release date: 2016-11-23, Last modification date: 2024-04-24)
Primary citationFischer, N.,Neumann, P.,Bock, L.V.,Maracci, C.,Wang, Z.,Paleskava, A.,Konevega, A.L.,Schroder, G.F.,Grubmuller, H.,Ficner, R.,Rodnina, M.V.,Stark, H.
The pathway to GTPase activation of elongation factor SelB on the ribosome.
Nature, 540:80-85, 2016
Cited by
PubMed Abstract: In all domains of life, selenocysteine (Sec) is delivered to the ribosome by selenocysteine-specific tRNA (tRNA) with the help of a specialized translation factor, SelB in bacteria. Sec-tRNA 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-tRNA binding by SelB and show large-scale rearrangements of Sec-tRNA. Upon initial binding of SelB-Sec-tRNA to the ribosome and codon reading, the 30S subunit adopts an open conformation with Sec-tRNA 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-tRNA 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.
PubMed: 27842381
DOI: 10.1038/nature20560
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.6 Å)
Structure validation

227111

數據於2024-11-06公開中

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