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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-9698 | |||||||||
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Title | NSF-D1D2 part in the whole 20S complex | |||||||||
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Function / homology | ![]() SNARE complex disassembly / ATP-dependent protein disaggregase activity / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Huang X / Sun S | |||||||||
![]() | ![]() Title: Mechanistic insights into the SNARE complex disassembly. Authors: Xuan Huang / Shan Sun / Xiaojing Wang / Fenghui Fan / Qiang Zhou / Shan Lu / Yong Cao / Qiu-Wen Wang / Meng-Qiu Dong / Jun Yao / Sen-Fang Sui / ![]() Abstract: NSF (-ethylmaleimide-sensitive factor) and α-SNAP (α-soluble NSF attachment protein) bind to the SNARE (soluble NSF attachment protein receptor) complex, the minimum machinery to mediate membrane ...NSF (-ethylmaleimide-sensitive factor) and α-SNAP (α-soluble NSF attachment protein) bind to the SNARE (soluble NSF attachment protein receptor) complex, the minimum machinery to mediate membrane fusion, to form a 20S complex, which disassembles the SNARE complex for reuse. We report the cryo-EM structures of the α-SNAP-SNARE subcomplex and the NSF-D1D2 domain in the 20S complex at 3.9- and 3.7-Å resolutions, respectively. Combined with the biochemical and electrophysiological analyses, we find that α-SNAPs use R116 through electrostatic interactions and L197 through hydrophobic interactions to apply force mainly on two positions of the VAMP protein to execute disassembly process. Furthermore, we define the interaction between the amino terminus of the SNARE helical bundle and the pore loop of the NSF-D1 domain and demonstrate its essential role as a potential anchor for SNARE complex disassembly. Our studies provide a rotation model of α-SNAP-mediated disassembly of the SNARE complex. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 14.6 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 9.7 KB 9.7 KB | Display Display | ![]() |
Images | ![]() | 192.4 KB | ||
Filedesc metadata | ![]() | 5.7 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6ip2MC ![]() 9697C ![]() 9723C ![]() 9724C ![]() 9725C ![]() 9726C ![]() 9727C ![]() 9728C ![]() 9729C ![]() 6ip1C M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.30654 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : NSF-D1D2 part in the whole 20S complex
Entire | Name: NSF-D1D2 part in the whole 20S complex |
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Components |
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-Supramolecule #1: NSF-D1D2 part in the whole 20S complex
Supramolecule | Name: NSF-D1D2 part in the whole 20S complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: ![]() ![]() ![]() |
-Macromolecule #1: Vesicle-fusing ATPase
Macromolecule | Name: Vesicle-fusing ATPase / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO / EC number: ![]() |
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Source (natural) | Organism: ![]() ![]() ![]() |
Molecular weight | Theoretical: 85.441133 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: MRGSHHHHHH TDPLDVDSEP DVSAKMAGRS MQAARCPTDE LSLSNCAVVS EKDYQSGQHV IVRTSPNHKY IFTLRTHPSV VPGSVAFSL PQRKWAGLSI GQEIEVALYS FDKAKQCIGT MTIEIDFLQK KNIDSNPYDT DKMAAEFIQQ FNNQAFSVGQ Q LVFSFNDK ...String: MRGSHHHHHH TDPLDVDSEP DVSAKMAGRS MQAARCPTDE LSLSNCAVVS EKDYQSGQHV IVRTSPNHKY IFTLRTHPSV VPGSVAFSL PQRKWAGLSI GQEIEVALYS FDKAKQCIGT MTIEIDFLQK KNIDSNPYDT DKMAAEFIQQ FNNQAFSVGQ Q LVFSFNDK LFGLLVKDIE AVDPSILKGE PASGKRQKIE VGLVVGNSQV AFEKAENSSL NLIGKAKTKE NRQSIINPDW NF EKMGIGG LDKEFSDIFR RAFASRVFPP EIVEQMGCKH VKGILLYGPP GCGKTLLARQ IGKMLNAREP KVVNGPEILN KYV GESEAN IRKLFADAEE EQRRLGANSG LHIIIFDEID AICKQRGSMA GSTGVHDTVV NQLLSKIDGV EQLNNILVIG MTNR PDLID EALLRPGRLE VKMEIGLPDE KGRLQILHIH TARMRGHQLL SADVDIKELA VETKNFSGAE LEGLVRAAQS TAMNR HIKA STKVEVDMEK AESLQVTRGD FLASLENDIK PAFGTNQEDY ASYIMNGIIK WGDPVTRVLD DGELLVQQTK NSDRTP LVS VLLEGPPHSG KTALAAKIAE ESNFPFIKIC SPDKMIGFSE TAKCQAMKKI FDDAYKSQLS CVVVDDIERL LDYVPIG PR FSNLVLQALL VLLKKAPPQG RKLLIIGTTS RKDVLQEMEM LNAFSTTIHV PNIATGEQLL EALELLGNFK DKERTTIA Q QVKGKKVWIG IKKLLMLIEM SLQMDPEYRV RKFLALLREE GASPLDFD UniProtKB: ![]() |
-Macromolecule #2: ADENOSINE-5'-TRIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 2 / Number of copies: 12 / Formula: ATP |
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Molecular weight | Theoretical: 507.181 Da |
Chemical component information | ![]() ChemComp-ATP: |
-Experimental details
-Structure determination
Method | ![]() |
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Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.4 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD![]() |
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 50.0 e/Å2 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: EMDB MAP |
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Initial angle assignment | Type: RANDOM ASSIGNMENT |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 163942 |