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3IYR

tmRNA-SmpB: a journey to the center of the bacterial ribosome

Summary for 3IYR
Entry DOI10.2210/pdb3iyr/pdb
Related3IYQ
EMDB information5189
DescriptortmRNA, SsrA-binding protein (2 entities in total)
Functional Keywordstmrna, smpb, ribosome, trans-translation, ribosomal protein-rna complex, ribosomal protein/rna
Biological sourceThermus thermophilus
More
Total number of polymer chains2
Total formula weight130302.12
Authors
Weis, F.,Bron, P.,Giudice, E.,Rolland, J.P.,Thomas, D.,Felden, B.,Gillet, R. (deposition date: 2010-04-16, release date: 2010-10-20, Last modification date: 2024-02-21)
Primary citationWeis, F.,Bron, P.,Giudice, E.,Rolland, J.P.,Thomas, D.,Felden, B.,Gillet, R.
tmRNA-SmpB: a journey to the centre of the bacterial ribosome.
Embo J., 29:3810-3818, 2010
Cited by
PubMed Abstract: Ribosomes mediate protein synthesis by decoding the information carried by messenger RNAs (mRNAs) and catalysing peptide bond formation between amino acids. When bacterial ribosomes stall on incomplete messages, the trans-translation quality control mechanism is activated by the transfer-messenger RNA bound to small protein B (tmRNA-SmpB ribonucleoprotein complex). Trans-translation liberates the stalled ribosomes and triggers degradation of the incomplete proteins. Here, we present the cryo-electron microscopy structures of tmRNA-SmpB accommodated or translocated into stalled ribosomes. Two atomic models for each state are proposed. This study reveals how tmRNA-SmpB crosses the ribosome and how, as the problematic mRNA is ejected, the tmRNA resume codon is placed onto the ribosomal decoding site by new contacts between SmpB and the nucleotides upstream of the tag-encoding sequence. This provides a structural basis for the transit of the large tmRNA-SmpB complex through the ribosome and for the means by which the tmRNA internal frame is set for translation to resume.
PubMed: 20953161
DOI: 10.1038/emboj.2010.252
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (13 Å)
Structure validation

226707

數據於2024-10-30公開中

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