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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Y20S (Sec18-Sec17-Sec9-Sso1-Snc1) EDTA - Class 1 | |||||||||
![]() | For overall placement of SNARE spire and Sec17 adaptor molecules | |||||||||
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![]() | SNARE / NSF / Sec18 / AAA+ / TRANSLOCASE | |||||||||
Function / homology | ![]() inter-Golgi cisterna vesicle-mediated transport / Disinhibition of SNARE formation / vesicle fusion to plasma membrane / ascospore-type prospore assembly / Retrograde transport at the Trans-Golgi-Network / RHOQ GTPase cycle / vesicle fusion with Golgi apparatus / RHOB GTPase cycle / RHOA GTPase cycle / Golgi vesicle fusion to target membrane ...inter-Golgi cisterna vesicle-mediated transport / Disinhibition of SNARE formation / vesicle fusion to plasma membrane / ascospore-type prospore assembly / Retrograde transport at the Trans-Golgi-Network / RHOQ GTPase cycle / vesicle fusion with Golgi apparatus / RHOB GTPase cycle / RHOA GTPase cycle / Golgi vesicle fusion to target membrane / sporulation / cellular bud / Intra-Golgi traffic / trans-Golgi Network Vesicle Budding / prospore membrane / soluble NSF attachment protein activity / ascospore formation / vacuole fusion, non-autophagic / COPI-dependent Golgi-to-ER retrograde traffic / COPI-mediated anterograde transport / COPII-mediated vesicle transport / SNARE complex disassembly / Golgi to endosome transport / vesicle docking / SNAP receptor activity / SNARE complex / phosphatidic acid binding / vesicle fusion / Golgi to plasma membrane transport / cellular bud neck / intra-Golgi vesicle-mediated transport / Golgi to plasma membrane protein transport / mating projection tip / Golgi stack / phosphatidylinositol-3,4-bisphosphate binding / fungal-type vacuole membrane / retrograde transport, endosome to Golgi / phosphatidylinositol-3,5-bisphosphate binding / syntaxin binding / SNARE complex assembly / transport vesicle membrane / exocytosis / ATPase activator activity / autophagosome assembly / endoplasmic reticulum to Golgi vesicle-mediated transport / phosphatidylinositol-4,5-bisphosphate binding / Neutrophil degranulation / endomembrane system / SNARE binding / cell periphery / macroautophagy / intracellular protein transport / trans-Golgi network / autophagy / endocytosis / molecular adaptor activity / endosome membrane / endosome / Golgi membrane / Golgi apparatus / ATP hydrolysis activity / ATP binding / plasma membrane / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.89 Å | |||||||||
![]() | Khan YA / Brunger AT | |||||||||
Funding support | ![]()
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![]() | ![]() Title: A conserved mechanism for universal SNARE recycling across cellular contexts Authors: Khan YA / Brunger AT | |||||||||
History |
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Structure visualization
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Downloads & links
-EMDB archive
Map data | ![]() | 76.1 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 28 KB 28 KB | Display Display | ![]() |
Images | ![]() | 64.5 KB | ||
Filedesc metadata | ![]() | 7.1 KB | ||
Others | ![]() ![]() ![]() ![]() ![]() | 48.6 MB 91.5 MB 91 MB 76.1 MB 76.1 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1 MB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 13.2 KB | Display | |
Data in CIF | ![]() | 15.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9cruMC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||
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Annotation | For overall placement of SNARE spire and Sec17 adaptor molecules | ||||||||||||||||||||
Voxel size | X=Y=Z: 1.096 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : Y20S complex EDTA
Entire | Name: Y20S complex EDTA |
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Components |
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-Supramolecule #1: Y20S complex EDTA
Supramolecule | Name: Y20S complex EDTA / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5 |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Vesicular-fusion protein SEC18
Macromolecule | Name: Vesicular-fusion protein SEC18 / type: protein_or_peptide / ID: 1 / Details: Cleaved Sec18 / Number of copies: 6 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 84.423297 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: GAHMFKIPGF GKAAANHTPP DMTNMDTRTR HLKVSNCPNN SYALANVAAV SPNDFPNNIY IIIDNLFVFT TRHSNDIPPG TIGFNGNQR TWGGWSLNQD VQAKAFDLFK YSGKQSYLGS IDIDISFRAR GKAVSTVFDQ DELAKQFVRC YESQIFSPTQ Y LIMEFQGH ...String: GAHMFKIPGF GKAAANHTPP DMTNMDTRTR HLKVSNCPNN SYALANVAAV SPNDFPNNIY IIIDNLFVFT TRHSNDIPPG TIGFNGNQR TWGGWSLNQD VQAKAFDLFK YSGKQSYLGS IDIDISFRAR GKAVSTVFDQ DELAKQFVRC YESQIFSPTQ Y LIMEFQGH FFDLKIRNVQ AIDLGDIEPT SAVATGIETK GILTKQTQIN FFKGRDGLVN LKSSNSLRPR SNAVIRPDFK FE DLGVGGL DKEFTKIFRR AFASRIFPPS VIEKLGISHV KGLLLYGPPG TGKTLIARKI GTMLNAKEPK IVNGPEILSK YVG SSEENI RNLFKDAEAE YRAKGEESSL HIIIFDELDS VFKQRGSRGD GTGVGDNVVN QLLAKMDGVD QLNNILVIGM TNRK DLIDS ALLRPGRFEV QVEIHLPDEK GRLQIFDIQT KKMRENNMMS DDVNLAELAA LTKNFSGAEI EGLVKSASSF AINKT VNIG KGATKLNTKD IAKLKVTRED FLNALNDVTP AFGISEEDLK TCVEGGMMLY SERVNSILKN GARYVRQVRE SDKSRL VSL LIHGPAGSGK TALAAEIALK SGFPFIRLIS PNELSGMSES AKIAYIDNTF RDAYKSPLNI LVIDSLETLV DWVPIGP RF SNNILQMLKV ALKRKPPQDR RLLIMTTTSA YSVLQQMDIL SCFDNEIAVP NMTNLDELNN VMIESNFLDD AGRVKVIN E LSRSCPNFNV GIKKTLTNIE TARHDEDPVN ELVELMTQSA UniProtKB: Vesicular-fusion protein SEC18 |
-Macromolecule #2: Alpha-soluble NSF attachment protein
Macromolecule | Name: Alpha-soluble NSF attachment protein / type: protein_or_peptide / ID: 2 / Details: TEV cleaved Sec17 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 32.899828 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: GMSDPVELLK RAEKKGVPSS GFMKLFSGSD SYKFEEAADL CVQAATIYRL RKELNLAGDS FLKAADYQKK AGNEDEAGNT YVEAYKCFK SGGNSVNAVD SLENAIQIFT HRGQFRRGAN FKFELGEILE NDLHDYAKAI DCYELAGEWY AQDQSVALSN K CFIKCADL ...String: GMSDPVELLK RAEKKGVPSS GFMKLFSGSD SYKFEEAADL CVQAATIYRL RKELNLAGDS FLKAADYQKK AGNEDEAGNT YVEAYKCFK SGGNSVNAVD SLENAIQIFT HRGQFRRGAN FKFELGEILE NDLHDYAKAI DCYELAGEWY AQDQSVALSN K CFIKCADL KALDGQYIEA SDIYSKLIKS SMGNRLSQWS LKDYFLKKGL CQLAATDAVA AARTLQEGQS EDPNFADSRE SN FLKSLID AVNEGDSEQL SEHCKEFDNF MRLDKWKITI LNKIKESIQQ QEDDLL UniProtKB: Alpha-soluble NSF attachment protein |
-Macromolecule #3: Synaptobrevin homolog 1
Macromolecule | Name: Synaptobrevin homolog 1 / type: protein_or_peptide / ID: 3 / Details: Snc1p TEV cleaved / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 10.943198 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: GASHMSSSTP FDPYALSEHD EERPQNVQSK SRTAELQAEI DDTVGIMRDN INKVAERGER LTSIEDKADN LAVSAQGFKR GANRVRKAM WYKDLKMK UniProtKB: Synaptobrevin homolog 1 |
-Macromolecule #4: Protein SSO1
Macromolecule | Name: Protein SSO1 / type: protein_or_peptide / ID: 4 / Details: Sso1 TEV cleaved / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 30.798027 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: GASHMSYNNP YQLETPFEES YELDEGSSAI GAEGHDFVGF MNKISQINRD LDKYDHTINQ VDSLHKRLLT EVNEEQASHL RHSLDNFVA QATDLQFKLK NEIKSAQRDG IHDTNKQAQA ENSRQRFLKL IQDYRIVDSN YKEENKEQAK RQYMIIQPEA T EDEVEAAI ...String: GASHMSYNNP YQLETPFEES YELDEGSSAI GAEGHDFVGF MNKISQINRD LDKYDHTINQ VDSLHKRLLT EVNEEQASHL RHSLDNFVA QATDLQFKLK NEIKSAQRDG IHDTNKQAQA ENSRQRFLKL IQDYRIVDSN YKEENKEQAK RQYMIIQPEA T EDEVEAAI SDVGGQQIFS QALLNANRRG EAKTALAEVQ ARHQELLKLE KSMAELTQLF NDMEELVIEQ QENVDVIDKN VE DAQLDVE QGVGHTDKAV KSARKARKNK IR UniProtKB: Protein SSO1 |
-Macromolecule #5: Protein transport protein SEC9
Macromolecule | Name: Protein transport protein SEC9 / type: protein_or_peptide / ID: 5 / Details: Sec9 TEV cleaved / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 25.77792 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: GASHIKFTKQ SSVASTRNTL KMAQDAERAG MNTLGMLGHQ SEQLNNVEGN LDLMKVQNKV ADEKVAELKK LNRSILAVHV SNPFNSKRR RREREEQLKN RKIEEKLMRE QTSQQLSQST QRIEGAMNAN NNISEVRERY QRKNVLEKAK RYQFENDEED D EMELEIDR ...String: GASHIKFTKQ SSVASTRNTL KMAQDAERAG MNTLGMLGHQ SEQLNNVEGN LDLMKVQNKV ADEKVAELKK LNRSILAVHV SNPFNSKRR RREREEQLKN RKIEEKLMRE QTSQQLSQST QRIEGAMNAN NNISEVRERY QRKNVLEKAK RYQFENDEED D EMELEIDR NLDQIQQVSN RLKKMALTTG KELDSQQKRL NNIEESTDDL DINLHMNTNR LAGI UniProtKB: Protein transport protein SEC9 |
-Macromolecule #6: ADENOSINE-5'-DIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 6 / Number of copies: 2 / Formula: ADP |
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Molecular weight | Theoretical: 427.201 Da |
Chemical component information | ![]() ChemComp-ADP: |
-Macromolecule #7: ADENOSINE-5'-TRIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 7 / Number of copies: 9 / Formula: ATP |
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Molecular weight | Theoretical: 507.181 Da |
Chemical component information | ![]() ChemComp-ATP: |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 0.8 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |