3J7Q

Structure of the idle mammalian ribosome-Sec61 complex

This is a non-PDB format compatible entry.

Replaces:  3J72Replaces:  1VWYReplaces:  1VWZ

Summary for 3J7Q

• Entry DOI: 10.2210/pdb3j7q/pdb
• Related: 3J7O 3J7P 3J7R
• EMDB information: 2644 2646 2649 2650
• Descriptor: 28S ribosomal RNA, Ribosomal protein eL8, Ribosomal protein uL6, ... (50 entities in total)
• Functional Keywords: mammalian, sec61, translocation, translation, ribosome
• Biological source: Sus scrofa (Pig); More
• Total number of polymer chains: 48
• Total formula weight: 2172228.42

Authors

Voorhees, R.M.,Fernandez, I.S.,Scheres, S.H.W.,Hegde, R.S. (deposition date: 2014-08-01, release date: 2014-09-03, Last modification date: 2024-10-16)

Primary citation

Voorhees, R.M.,Fernandez, I.S.,Scheres, S.H.,Hegde, R.S.
Structure of the Mammalian ribosome-sec61 complex to 3.4 a resolution.
Cell(Cambridge,Mass.), 157:1632-1643, 2014

PubMed 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.

PubMed: 24930395
DOI: 10.1016/j.cell.2014.05.024

Experimental method

ELECTRON MICROSCOPY (3.4 Å)