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Structure of the mammalian ribosome-Sec61 complex to 3.4 Å resolution.

<div class='caption-title'>The Structure of a Mammalian Ribosome-Translocon Complex</div>
<div class='caption-title'>Representative Density for the Ribosomal Proteins and rRNA</div>
<div class='caption-title'>An A/P Hybrid State tRNA</div>
Voorhees RM, Fernández IS, Scheres SH, Hegde RS
OpenAccess logo Cell 157 1632-43 (2014)
Related entries: 3j7o, 3j7p, 3j7r

Cited: 224 times
EuropePMC logo PMID: 24930395

Abstract

Cotranslational protein translocation is a universally conserved process for secretory and membrane protein biosynthesis. Nascent polypeptides emerging from a translating ribosome are either transported across or inserted into the membrane via the ribosome-bound Sec61 channel. Here, we report structures of a mammalian ribosome-Sec61 complex in both idle and translating states, determined to 3.4 and 3.9 Å resolution. The data sets permit building of a near-complete atomic model of the mammalian ribosome, visualization of A/P and P/E hybrid-state tRNAs, and analysis of a nascent polypeptide in the exit tunnel. Unprecedented chemical detail is observed for both the ribosome-Sec61 interaction and the conformational state of Sec61 upon ribosome binding. Comparison of the maps from idle and translating complexes suggests how conformational changes to the Sec61 channel could facilitate translocation of a secreted polypeptide. The high-resolution structure of the mammalian ribosome-Sec61 complex provides a valuable reference for future functional and structural studies.

Reviews - 3j7q mentioned but not cited (5)

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  5. Molecular Modeling of Signal Peptide Recognition by Eukaryotic Sec Complexes. Bhadra P, Helms V. Int J Mol Sci 22 10705 (2021)

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