3iyr | pdb_00003iyr

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

Loading... Status: waiting for Mol* initialization Structural highlights 3iyr is a 2 chain structure with sequence from Thermus thermophilus HB8. The January 2013 RCSB PDB Molecule of the Month feature on Transfer-Messenger RNA by David Goodsell is 10.2210/rcsb_pdb/mom_2013_1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 13Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SSRP_THET8 Binds specifically to the SsrA RNA (tmRNA) and is required for stable association of SsrA with ribosomes (By similarity). Publication Abstract from PubMed 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. tmRNA-SmpB: a journey to the centre of the bacterial ribosome.,Weis F, Bron P, Giudice E, Rolland JP, Thomas D, Felden B, Gillet R EMBO J. 2010 Nov 17;29(22):3810-8. Epub 2010 Oct 15. PMID:20953161 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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