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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Asgard ESCRT-IIIB membrane-bound protofilament structure | |||||||||
![]() | Postprocessed map of membrane-decorated Asgard ESCRT-IIIB | |||||||||
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![]() | ESCRT-III / filament / membrane binding protein / membrane remodeling / Asgard archaea / MEMBRANE PROTEIN | |||||||||
Function / homology | Snf7 family / Snf7 / late endosome to vacuole transport via multivesicular body sorting pathway / vesicle budding from membrane / endomembrane system / cytoplasmic side of plasma membrane / intracellular membrane-bounded organelle / Uncharacterized protein![]() | |||||||||
Biological species | ![]() | |||||||||
Method | helical reconstruction / cryo EM / Resolution: 6.5 Å | |||||||||
![]() | Chaaban S / Souza DP / Baum B | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Asgard archaea reveal the conserved principles of ESCRT-III membrane remodeling. Authors: Diorge P Souza / Javier Espadas / Sami Chaaban / Edmund R R Moody / Tomoyuki Hatano / Mohan Balasubramanian / Tom A Williams / Aurélien Roux / Buzz Baum / ![]() ![]() Abstract: ESCRT-III proteins assemble into composite polymers that undergo stepwise changes in composition and structure to deform membranes across the tree of life. Here, using a phylogenetic analysis, we ...ESCRT-III proteins assemble into composite polymers that undergo stepwise changes in composition and structure to deform membranes across the tree of life. Here, using a phylogenetic analysis, we demonstrate that the two endosomal sorting complex required for transport III (ESCRT-III) proteins present in eukaryote's closest Asgard archaeal relatives are evolutionarily related to the B- and A-type eukaryotic paralogs that initiate and execute membrane remodeling, respectively. We show that Asgard ESCRT-IIIB assembles into parallel arrays on planar membranes to initiate membrane deformation, from where it recruits ESCRT-IIIA to generate composite polymers. Last, we show that Asgard ESCRT-IIIA is able to remodel membranes into tubes as a likely prelude to scission. Together, these data reveal a set of conserved principles governing ESCRT-III-dependent membrane remodeling that first emerged in a two-component ESCRT-III system in archaea. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 26.4 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 19.5 KB 19.5 KB | Display Display | ![]() |
Images | ![]() | 178.2 KB | ||
Masks | ![]() | 78.5 MB | ![]() | |
Filedesc metadata | ![]() | 6.1 KB | ||
Others | ![]() ![]() ![]() | 72.6 MB 61.2 MB 61.2 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9ftmMC ![]() 9ftlC 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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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||
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Annotation | Postprocessed map of membrane-decorated Asgard ESCRT-IIIB | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.5073 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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Projections & Slices |
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Density Histograms |
-Additional map: Unprocessed map membrane-decorated Asgard ESCRT-IIIB
File | emd_50749_additional_1.map | ||||||||||||
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Annotation | Unprocessed map membrane-decorated Asgard ESCRT-IIIB | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half-map 1 of membrane-decorated Asgard ESCRT-IIIB
File | emd_50749_half_map_1.map | ||||||||||||
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Annotation | Half-map 1 of membrane-decorated Asgard ESCRT-IIIB | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half-map 2 of membrane-decorated Asgard ESCRT-IIIB
File | emd_50749_half_map_2.map | ||||||||||||
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Annotation | Half-map 2 of membrane-decorated Asgard ESCRT-IIIB | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Membrane-bound Asgard ESCRT-IIIB protofilament array
Entire | Name: Membrane-bound Asgard ESCRT-IIIB protofilament array |
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Components |
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-Supramolecule #1: Membrane-bound Asgard ESCRT-IIIB protofilament array
Supramolecule | Name: Membrane-bound Asgard ESCRT-IIIB protofilament array / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 33 kDa/nm |
-Macromolecule #1: Heimdallarchaeota archaeon AB_125 ESCRT-IIIB
Macromolecule | Name: Heimdallarchaeota archaeon AB_125 ESCRT-IIIB / type: protein_or_peptide / ID: 1 / Number of copies: 8 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 24.130268 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MVKNWLFGKK RKEDADALAT LKGQQNRLQA EARNLERQSD EQKILASKML KAGNKAGARQ ALKRRAVFMK RLNTVHNTAM NLQAQIDSI QTATSTAETV KAMELGTKVV GEKIKTVSPE RTERVMDSVM EQRDQIEMMT EALSDPSLSE GILDFEDDAA I DEQLAQLE ...String: MVKNWLFGKK RKEDADALAT LKGQQNRLQA EARNLERQSD EQKILASKML KAGNKAGARQ ALKRRAVFMK RLNTVHNTAM NLQAQIDSI QTATSTAETV KAMELGTKVV GEKIKTVSPE RTERVMDSVM EQRDQIEMMT EALSDPSLSE GILDFEDDAA I DEQLAQLE AEMDLGTTTS LPDVSGLPST PVGTGEKEED TSELEAELEG LKKKMSEDKQ UniProtKB: Uncharacterized protein |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | helical reconstruction |
Aggregation state | filament |
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Sample preparation
Concentration | 0.5 mg/mL |
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Buffer | pH: 6 / Component - Concentration: 20.0 mM / Component - Formula: Bis-Tris-HCl / Component - Name: Bis-Tris-HCl Details: 20 mM Bis-Tris-HCl pH 6.0, 0.12 mM 1,2-dioleoyl-sn-glycero-3-phosphocholine, 0.08 mM 1,2-dioleoyl-sn-glycero-3-phospho-L-serine |
Grid | Model: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 12 sec. |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 293.15 K / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Number real images: 29600 / 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: 2.6 µm / Nominal defocus min: 0.6 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Final reconstruction | Applied symmetry - Helical parameters - Δz: 29.9 Å Applied symmetry - Helical parameters - Δ&Phi: 0.4 ° Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric) Resolution.type: BY AUTHOR / Resolution: 6.5 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 5) / Number images used: 27747 |
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Startup model | Type of model: NONE / Details: Ab initio |
Final angle assignment | Type: NOT APPLICABLE / Software - Name: RELION (ver. 5) |
-Atomic model buiding 1
Initial model | Chain - Source name: Other / Chain - Initial model type: experimental model Details: The initial model was obtained from the high resolution four-protofilament structure off membranes |
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Refinement | Space: REAL / Protocol: FLEXIBLE FIT |
Output model | ![]() PDB-9ftm: |