6W6L
Cryo-EM structure of the human ribosome-TMCO1 translocon
This is a non-PDB format compatible entry.
Summary for 6W6L
Entry DOI | 10.2210/pdb6w6l/pdb |
EMDB information | 21426 21427 21435 |
Descriptor | 60S ribosomal protein L8, 60S ribosomal protein L9, 60S ribosomal protein L10, ... (57 entities in total) |
Functional Keywords | ribosome-protein transport complex, ribosome/protein transport |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 54 |
Total formula weight | 2349794.40 |
Authors | Keenan, R.J.,McGilvray, P.T. (deposition date: 2020-03-17, release date: 2020-09-02, Last modification date: 2024-11-13) |
Primary citation | McGilvray, P.T.,Anghel, S.A.,Sundaram, A.,Zhong, F.,Trnka, M.J.,Fuller, J.R.,Hu, H.,Burlingame, A.L.,Keenan, R.J. An ER translocon for multi-pass membrane protein biogenesis. Elife, 9:-, 2020 Cited by PubMed Abstract: Membrane proteins with multiple transmembrane domains play critical roles in cell physiology, but little is known about the machinery coordinating their biogenesis at the endoplasmic reticulum. Here we describe a ~ 360 kDa ribosome-associated complex comprising the core Sec61 channel and five accessory factors: TMCO1, CCDC47 and the Nicalin-TMEM147-NOMO complex. Cryo-electron microscopy reveals a large assembly at the ribosome exit tunnel organized around a central membrane cavity. Similar to protein-conducting channels that facilitate movement of transmembrane segments, cytosolic and luminal funnels in TMCO1 and TMEM147, respectively, suggest routes into the central membrane cavity. High-throughput mRNA sequencing shows selective translocon engagement with hundreds of different multi-pass membrane proteins. Consistent with a role in multi-pass membrane protein biogenesis, cells lacking different accessory components show reduced levels of one such client, the glutamate transporter EAAT1. These results identify a new human translocon and provide a molecular framework for understanding its role in multi-pass membrane protein biogenesis. PubMed: 32820719DOI: 10.7554/eLife.56889 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.84 Å) |
Structure validation
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