8FTU
Crystal structure of the SNARE Use1 bound to Dsl1 complex subunits Sec39 and Dsl1, Revised Use1 structure
Replaces: 6WC4Summary for 8FTU
| Entry DOI | 10.2210/pdb8ftu/pdb |
| Related | 6WC4 |
| Descriptor | Protein transport protein SEC39, Vesicle transport protein USE1, Protein transport protein DSL1 (3 entities in total) |
| Functional Keywords | membrane trafficking, snare protein, copi, vesicle, multisubunit tethering complex, dsl1 complex, catchr complex, transport protein |
| Biological source | Kluyveromyces lactis NRRL Y-1140 More |
| Total number of polymer chains | 3 |
| Total formula weight | 129135.87 |
| Authors | Travis, S.M.,Jeffrey, P.D.,Hughson, F.M. (deposition date: 2023-01-13, release date: 2023-03-01, Last modification date: 2024-02-28) |
| Primary citation | DAmico, K.A.,Stanton, A.E.,Shirkey, J.D.,Travis, S.M.,Jeffrey, P.D.,Hughson, F.M. Structure of a membrane tethering complex incorporating multiple SNAREs. Nat.Struct.Mol.Biol., 31:246-254, 2024 Cited by PubMed Abstract: Most membrane fusion reactions in eukaryotic cells are mediated by multisubunit tethering complexes (MTCs) and SNARE proteins. MTCs are much larger than SNAREs and are thought to mediate the initial attachment of two membranes. Complementary SNAREs then form membrane-bridging complexes whose assembly draws the membranes together for fusion. Here we present a cryo-electron microscopy structure of the simplest known MTC, the 255-kDa Dsl1 complex of Saccharomyces cerevisiae, bound to the two SNAREs that anchor it to the endoplasmic reticulum. N-terminal domains of the SNAREs form an integral part of the structure, stabilizing a Dsl1 complex configuration with unexpected similarities to the 850-kDa exocyst MTC. The structure of the SNARE-anchored Dsl1 complex and its comparison with exocyst reveal what are likely to be common principles underlying MTC function. Our structure also implies that tethers and SNAREs can work together as a single integrated machine. PubMed: 38196032DOI: 10.1038/s41594-023-01164-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (5.73 Å) |
Structure validation
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