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Title | Cryo-EM structure of SNAP-SNARE assembly in 20S particle. |
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Journal, issue, pages | Cell Res, Vol. 25, Issue 5, Page 551-560, Year 2015 |
Publish date | Apr 24, 2015 |
Authors | Qiang Zhou / Xuan Huang / Shan Sun / Xueming Li / Hong-Wei Wang / Sen-Fang Sui / |
PubMed Abstract | N-ethylmaleimide-sensitive factor (NSF) and α soluble NSF attachment proteins (α-SNAPs) work together within a 20S particle to disassemble and recycle the SNAP receptor (SNARE) complex after ...N-ethylmaleimide-sensitive factor (NSF) and α soluble NSF attachment proteins (α-SNAPs) work together within a 20S particle to disassemble and recycle the SNAP receptor (SNARE) complex after intracellular membrane fusion. To understand the disassembly mechanism of the SNARE complex by NSF and α-SNAP, we performed single-particle cryo-electron microscopy analysis of 20S particles and determined the structure of the α-SNAP-SNARE assembly portion at a resolution of 7.35 Å. The structure illustrates that four α-SNAPs wrap around the single left-handed SNARE helical bundle as a right-handed cylindrical assembly within a 20S particle. A conserved hydrophobic patch connecting helices 9 and 10 of each α-SNAP forms a chock protruding into the groove of the SNARE four-helix bundle. Biochemical studies proved that this structural element was critical for SNARE complex disassembly. Our study suggests how four α-SNAPs may coordinate with the NSF to tear the SNARE complex into individual proteins. |
External links | Cell Res / PubMed:25906996 / PubMed Central |
Methods | EM (single particle) |
Resolution | 7.35 Å |
Structure data | EMDB-2874: |
Source |
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