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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 | |||||||||
Map data | Postprocessed map of membrane-decorated Asgard ESCRT-IIIB | |||||||||
Sample |
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Keywords | 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 Function and homology information | |||||||||
| Biological species | Candidatus Heimdallarchaeota archaeon (archaea) | |||||||||
| Method | helical reconstruction / cryo EM / Resolution: 6.5 Å | |||||||||
Authors | Chaaban S / Souza DP / Baum B | |||||||||
| Funding support | United Kingdom, 2 items
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Citation | Journal: Sci Adv / Year: 2025Title: 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. | |||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_50749.map.gz | 26.4 MB | EMDB map data format | |
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| Header (meta data) | emd-50749-v30.xml emd-50749.xml | 19.5 KB 19.5 KB | Display Display | EMDB header |
| Images | emd_50749.png | 178.2 KB | ||
| Masks | emd_50749_msk_1.map | 78.5 MB | Mask map | |
| Filedesc metadata | emd-50749.cif.gz | 6.1 KB | ||
| Others | emd_50749_additional_1.map.gz emd_50749_half_map_1.map.gz emd_50749_half_map_2.map.gz | 72.6 MB 61.2 MB 61.2 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-50749 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-50749 | HTTPS FTP |
-Validation report
| Summary document | emd_50749_validation.pdf.gz | 829.8 KB | Display | EMDB validaton report |
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| Full document | emd_50749_full_validation.pdf.gz | 829.3 KB | Display | |
| Data in XML | emd_50749_validation.xml.gz | 12.7 KB | Display | |
| Data in CIF | emd_50749_validation.cif.gz | 15.1 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-50749 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-50749 | 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 F&H Search |
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_50749.map.gz / Format: CCP4 / Size: 78.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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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
| File | emd_50749_msk_1.map | ||||||||||||
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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 | ||||||||||||
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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 | ||||||||||||
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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: Candidatus Heimdallarchaeota archaeon (archaea) |
| 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: Candidatus Heimdallarchaeota archaeon (archaea) |
| 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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Processing | 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: FIELD EMISSION GUN |
| 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: |
Movie
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About Yorodumi




Keywords
Candidatus Heimdallarchaeota archaeon (archaea)
Authors
United Kingdom, 2 items
Citation



Z (Sec.)
Y (Row.)
X (Col.)





















































FIELD EMISSION GUN
