3KYQ
Lipid-induced Conformational Switch Controls Fusion Activity of Longin Domain SNARE Ykt6
Summary for 3KYQ
| Entry DOI | 10.2210/pdb3kyq/pdb |
| Descriptor | Synaptobrevin homolog YKT6, SULFATE ION, dodecyl 2-(trimethylammonio)ethyl phosphate, ... (4 entities in total) |
| Functional Keywords | v-snare homolog, lipid binding, cytoplasmic vesicle, er-golgi transport, golgi apparatus, lipoprotein, palmitate, prenylation, protein transport, transferase, transport |
| Biological source | Rattus norvegicus (Rat) |
| Cellular location | Cytoplasm, cytosol: Q5EGY4 |
| Total number of polymer chains | 1 |
| Total formula weight | 23055.24 |
| Authors | Yu, J.,Wen, W.Y.,Zhang, M.J. (deposition date: 2009-12-07, release date: 2010-03-02, Last modification date: 2023-11-01) |
| Primary citation | Wen, W.Y.,Yu, J.,Pan, L.F.,Wei, Z.Y.,Weng, J.W.,Wang, W.N.,Ong, Y.S.,Tran, T.H.T.,Hong, W.J.,Zhang, M.J. Lipid-Induced Conformational Switch Controls Fusion Activity of Longin Domain SNARE Ykt6 Mol.Cell, 37:383-395, 2010 Cited by PubMed Abstract: While most SNAREs are permanently anchored to membranes by their transmembrane domains, the dually lipidated SNARE Ykt6 is found both on intracellular membranes and in the cytosol. The cytosolic Ykt6 is inactive due to the autoinhibition of the SNARE core by its longin domain, although the molecular basis of this inhibition is unknown. Here, we demonstrate that unlipidated Ykt6 adopts multiple conformations, with a small population in the closed state. The structure of Ykt6 in complex with a fatty acid suggests that, upon farnesylation, the Ykt6 SNARE core forms four alpha helices that wrap around the longin domain, forming a dominantly closed conformation. The fatty acid, buried in a hydrophobic groove formed between the longin domain and its SNARE core, is essential for maintaining the autoinhibited conformation of Ykt6. Our study reveals that the posttranslationally attached farnesyl group can actively regulate Ykt6 fusion activity in addition to its anticipated membrane-anchoring role. PubMed: 20159557DOI: 10.1016/j.molcel.2010.01.024 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.443 Å) |
Structure validation
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