3JC2
The structure of the mammalian Sec61 channel opened by a signal sequence
Summary for 3JC2
| Entry DOI | 10.2210/pdb3jc2/pdb |
| EMDB information | 3245 |
| Descriptor | Protein transport protein Sec61 subunit alpha isoform 1, Protein transport protein Sec61 subunit gamma, Prolactin, ... (4 entities in total) |
| Functional Keywords | sec61, translocation, signal sequence, transport protein |
| Biological source | Bos taurus (bovine) More |
| Total number of polymer chains | 4 |
| Total formula weight | 64093.78 |
| Authors | Voorhees, R.M.,Hegde, R.S. (deposition date: 2015-11-15, release date: 2016-01-13, Last modification date: 2025-03-26) |
| Primary citation | Voorhees, R.M.,Hegde, R.S. Structure of the Sec61 channel opened by a signal sequence. Science, 351:88-91, 2016 Cited by PubMed Abstract: Secreted and integral membrane proteins compose up to one-third of the biological proteome. These proteins contain hydrophobic signals that direct their translocation across or insertion into the lipid bilayer by the Sec61 protein-conducting channel. The molecular basis of how hydrophobic signals within a nascent polypeptide trigger channel opening is not understood. Here, we used cryo-electron microscopy to determine the structure of an active Sec61 channel that has been opened by a signal sequence. The signal supplants helix 2 of Sec61α, which triggers a rotation that opens the central pore both axially across the membrane and laterally toward the lipid bilayer. Comparisons with structures of Sec61 in other states suggest a pathway for how hydrophobic signals engage the channel to gain access to the lipid bilayer. PubMed: 26721998DOI: 10.1126/science.aad4992 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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