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Open data
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Basic information
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Title | Architecture of the ESCPE-1 membrane coat | |||||||||
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![]() | sorting nexins / ![]() ![]() ![]() ![]() ![]() | |||||||||
Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | subtomogram averaging / ![]() | |||||||||
![]() | Lopez-Robles C / Scaramuzza S / Astorga-Simon E / Ishida M / Williamsom CD / Banos-Mateos S / Gil-Carton D / Romero M / Vidaurrazaga A / Fernandez-Recio J ...Lopez-Robles C / Scaramuzza S / Astorga-Simon E / Ishida M / Williamsom CD / Banos-Mateos S / Gil-Carton D / Romero M / Vidaurrazaga A / Fernandez-Recio J / Rojas AL / Bonifacino JS / Castano-Diez D / Hierro A | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Architecture of the ESCPE-1 membrane coat. Authors: Carlos Lopez-Robles / Stefano Scaramuzza / Elsa N Astorga-Simon / Morié Ishida / Chad D Williamson / Soledad Baños-Mateos / David Gil-Carton / Miguel Romero-Durana / Ander Vidaurrazaga / ...Authors: Carlos Lopez-Robles / Stefano Scaramuzza / Elsa N Astorga-Simon / Morié Ishida / Chad D Williamson / Soledad Baños-Mateos / David Gil-Carton / Miguel Romero-Durana / Ander Vidaurrazaga / Juan Fernandez-Recio / Adriana L Rojas / Juan S Bonifacino / Daniel Castaño-Díez / Aitor Hierro / ![]() ![]() ![]() Abstract: Recycling of membrane proteins enables the reuse of receptors, ion channels and transporters. A key component of the recycling machinery is the endosomal sorting complex for promoting exit 1 (ESCPE-1) ...Recycling of membrane proteins enables the reuse of receptors, ion channels and transporters. A key component of the recycling machinery is the endosomal sorting complex for promoting exit 1 (ESCPE-1), which rescues transmembrane proteins from the endolysosomal pathway for transport to the trans-Golgi network and the plasma membrane. This rescue entails the formation of recycling tubules through ESCPE-1 recruitment, cargo capture, coat assembly and membrane sculpting by mechanisms that remain largely unknown. Herein, we show that ESCPE-1 has a single-layer coat organization and suggest how synergistic interactions between ESCPE-1 protomers, phosphoinositides and cargo molecules result in a global arrangement of amphipathic helices to drive tubule formation. Our results thus define a key process of tubule-based endosomal sorting. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 3.1 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 18 KB 18 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 3.7 KB | Display | ![]() |
Images | ![]() | 161.3 KB | ||
Others | ![]() ![]() | 3.1 MB 3.1 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8afzMC ![]() 8a1gC ![]() 8abqC 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
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 2.73 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_15413_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_15413_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Endosomal Sorting Complex for Promoting Exit 1 (ESCPE-1)
Entire | Name: Endosomal Sorting Complex for Promoting Exit 1 (ESCPE-1) |
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Components |
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-Supramolecule #1: Endosomal Sorting Complex for Promoting Exit 1 (ESCPE-1)
Supramolecule | Name: Endosomal Sorting Complex for Promoting Exit 1 (ESCPE-1) type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 110 KDa |
-Macromolecule #1: Sorting nexin-1
Macromolecule | Name: Sorting nexin-1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 59.14434 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: MASGGGGCSA SERLPPPFPG LEPESEGAAG GSEPEAGDSD TEGEDIFTGA AVVSKHQSPK ITTSLLPINN GSKENGIHEE QDQEPQDLF ADATVELSLD STQNNQKKVL AKTLISLPPQ EATNSSKPQP TYEELEEEEQ EDQFDLTVGI TDPEKIGDGM N AYVAYKVT ...String: MASGGGGCSA SERLPPPFPG LEPESEGAAG GSEPEAGDSD TEGEDIFTGA AVVSKHQSPK ITTSLLPINN GSKENGIHEE QDQEPQDLF ADATVELSLD STQNNQKKVL AKTLISLPPQ EATNSSKPQP TYEELEEEEQ EDQFDLTVGI TDPEKIGDGM N AYVAYKVT TQTSLPLFRS KQFAVKRRFS DFLGLYEKLS EKHSQNGFIV PPPPEKSLIG MTKVKVGKED SSSAEFLEKR RA ALERYLQ RIVNHPTMLQ DPDVREFLEK EELPRAVGTQ TLSGAGLLKM FNKATDAVSK MTIKMNESDI WFEEKLQEVE CEE QRLRKL HAVVETLVNH RKELALNTAQ FAKSLAMLGS SEDNTALSRA LSQLAEVEEK IEQLHQEQAN NDFFLLAELL SDYI RLLAI VRAAFDQRMK TWQRWQDAQA TLQKKREAEA RLLWANKPDK LQQAKDEILE WESRVTQYER DFERISTVVR KEVIR FEKE KSKDFKNHVI KYLETLLYSQ QQLAKYWEAF LPEAKAIS UniProtKB: ![]() |
-Macromolecule #2: Sorting nexin-5
Macromolecule | Name: Sorting nexin-5 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 46.891504 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: MAAVPELLQQ QEEDRSKLRS VSVDLNVDPS LQIDIPDALS ERDKVKFTVH TKTTLPTFQS PEFSVTRQHE DFVWLHDTLI ETTDYAGLI IPPAPTKPDF DGPREKMQKL GEGEGSMTKE EFAKMKQELE AEYLAVFKKT VSSHEVFLQR LSSHPVLSKD R NFHVFLEY ...String: MAAVPELLQQ QEEDRSKLRS VSVDLNVDPS LQIDIPDALS ERDKVKFTVH TKTTLPTFQS PEFSVTRQHE DFVWLHDTLI ETTDYAGLI IPPAPTKPDF DGPREKMQKL GEGEGSMTKE EFAKMKQELE AEYLAVFKKT VSSHEVFLQR LSSHPVLSKD R NFHVFLEY DQDLSVRRKN TKEMFGGFFK SVVKSADEVL FTGVKEVDDF FEQEKNFLIN YYNRIKDSCV KADKMTRSHK NV ADDYIHT AACLHSLALE EPTVIKKYLL KVAELFEKLR KVEGRVSSDE DLKLTELLRY YMLNIEAAKD LLYRRTKALI DYE NSNKAL DKARLKSKDV KLAEAHQQEC CQKFEQLSES AKEELINFKR KRVAAFRKNL IEMSELEIKH ARNNVSLLQS CIDL FKNN UniProtKB: ![]() |
-Macromolecule #3: Cation-independent mannose-6-phosphate receptor
Macromolecule | Name: Cation-independent mannose-6-phosphate receptor / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 3.766033 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: SNVSYKYSKV NKEEETDENE TEWLMEEIQL P UniProtKB: Cation-independent mannose-6-phosphate receptor |
-Experimental details
-Structure determination
Method | ![]() |
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![]() | subtomogram averaging |
Aggregation state | particle |
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Sample preparation
Concentration | 3.0 mg/mL |
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Buffer | pH: 7.5 |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 90 % / Chamber temperature: 282 K / Instrument: FEI VITROBOT MARK II / Details: Incubation time 30s Blotting time 2s. |
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Electron microscopy
Microscope | TFS KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD![]() |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Number grids imaged: 1 / Average electron dose: 2.8 e/Å2 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |