8BTK
Structure of the TRAP complex with the Sec translocon and a translating ribosome
This is a non-PDB format compatible entry.
Summary for 8BTK
| Entry DOI | 10.2210/pdb8btk/pdb |
| EMDB information | 16232 |
| Descriptor | 28S rRNA, 60S ribosomal protein L7a, 60S ribosomal protein L9, ... (98 entities in total) |
| Functional Keywords | er targeting, protein translocation, er protein biogenesis, translocase |
| Biological source | Saccharomyces cerevisiae More |
| Total number of polymer chains | 92 |
| Total formula weight | 4037976.00 |
| Authors | Jaskolowski, M.,Jomaa, A.,Gamerdinger, M.,Shrestha, S.,Leibundgut, M.,Deuerling, E.,Ban, N. (deposition date: 2022-11-29, release date: 2023-05-24, Last modification date: 2024-04-24) |
| Primary citation | Jaskolowski, M.,Jomaa, A.,Gamerdinger, M.,Shrestha, S.,Leibundgut, M.,Deuerling, E.,Ban, N. Molecular basis of the TRAP complex function in ER protein biogenesis. Nat.Struct.Mol.Biol., 30:770-777, 2023 Cited by PubMed Abstract: The translocon-associated protein (TRAP) complex resides in the endoplasmic reticulum (ER) membrane and interacts with the Sec translocon and the ribosome to facilitate biogenesis of secretory and membrane proteins. TRAP plays a key role in the secretion of many hormones, including insulin. Here we reveal the molecular architecture of the mammalian TRAP complex and how it engages the translating ribosome associated with Sec61 translocon on the ER membrane. The TRAP complex is anchored to the ribosome via a long tether and its position is further stabilized by a finger-like loop. This positions a cradle-like lumenal domain of TRAP below the translocon for interactions with translocated nascent chains. Our structure-guided TRAP mutations in Caenorhabditis elegans lead to growth deficits associated with increased ER stress and defects in protein hormone secretion. These findings elucidate the molecular basis of the TRAP complex in the biogenesis and translocation of proteins at the ER. PubMed: 37170030DOI: 10.1038/s41594-023-00990-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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