+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-42926 | |||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Title | Cellular CHMP1B/IST1 filament - Class Id | |||||||||||||||||||||
Map data | Refined symmetrized sharpened map | |||||||||||||||||||||
Sample |
| |||||||||||||||||||||
Keywords | nucleic acid binding protein / cytoplasmic / HeLa / CHMP1B / IST1 / nucleic acids / CYTOSOLIC PROTEIN | |||||||||||||||||||||
Function / homology | Function and homology information MIT domain binding / abscission / multivesicular body-lysosome fusion / amphisome membrane / vesicle fusion with vacuole / ESCRT III complex disassembly / late endosome to lysosome transport / ESCRT III complex / kinetochore microtubule / cytoskeleton-dependent cytokinesis ...MIT domain binding / abscission / multivesicular body-lysosome fusion / amphisome membrane / vesicle fusion with vacuole / ESCRT III complex disassembly / late endosome to lysosome transport / ESCRT III complex / kinetochore microtubule / cytoskeleton-dependent cytokinesis / endosome transport via multivesicular body sorting pathway / collateral sprouting / regulation of centrosome duplication / nuclear membrane reassembly / positive regulation of collateral sprouting / Sealing of the nuclear envelope (NE) by ESCRT-III / midbody abscission / multivesicular body sorting pathway / membrane coat / plasma membrane repair / membrane fission / late endosome to vacuole transport / ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / multivesicular body membrane / multivesicular body assembly / regulation of mitotic spindle assembly / Flemming body / mitotic metaphase chromosome alignment / nucleus organization / viral budding via host ESCRT complex / endoplasmic reticulum-Golgi intermediate compartment / positive regulation of proteolysis / autophagosome membrane / autophagosome maturation / nuclear pore / multivesicular body / viral budding from plasma membrane / establishment of protein localization / kinetochore / autophagy / azurophil granule lumen / protein transport / protein localization / nuclear envelope / midbody / endosome membrane / cadherin binding / protein domain specific binding / lysosomal membrane / cell division / intracellular membrane-bounded organelle / centrosome / Neutrophil degranulation / protein-containing complex binding / chromatin / extracellular exosome / extracellular region / nucleoplasm / identical protein binding / plasma membrane / cytosol Similarity search - Function | |||||||||||||||||||||
Biological species | Homo sapiens (human) | |||||||||||||||||||||
Method | helical reconstruction / cryo EM / Resolution: 4.27 Å | |||||||||||||||||||||
Authors | Talledge N / Laughlin TG / Alian A / McCullough J | |||||||||||||||||||||
Funding support | United States, 6 items
| |||||||||||||||||||||
Citation | Journal: To Be Published Title: ESCRT-III Assembles Around Mis-segregated DNA to Engage NoCut Authors: Talledge N / Glover J / McCullough J / Alian A / Sadler JBA / Dempsey N / Laughlin TG / Nguyen HC / Wenzel D / Lalonde MS / Ventimiglia LN / LaJoie D / Iwasa J / Starling T / Padilla-Parra S ...Authors: Talledge N / Glover J / McCullough J / Alian A / Sadler JBA / Dempsey N / Laughlin TG / Nguyen HC / Wenzel D / Lalonde MS / Ventimiglia LN / LaJoie D / Iwasa J / Starling T / Padilla-Parra S / Ullman KS / Frost A / Sundquist WI / Martin-Serrano J | |||||||||||||||||||||
History |
|
-Structure visualization
Supplemental images |
---|
-Downloads & links
-EMDB archive
Map data | emd_42926.map.gz | 36.9 MB | EMDB map data format | |
---|---|---|---|---|
Header (meta data) | emd-42926-v30.xml emd-42926.xml | 28.4 KB 28.4 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_42926_fsc.xml | 9.5 KB | Display | FSC data file |
Images | emd_42926.png | 80.9 KB | ||
Masks | emd_42926_msk_1.map emd_42926_msk_2.map | 91.1 MB 91.1 MB | Mask map | |
Filedesc metadata | emd-42926.cif.gz | 6.5 KB | ||
Others | emd_42926_additional_1.map.gz emd_42926_additional_2.map.gz emd_42926_additional_3.map.gz emd_42926_half_map_1.map.gz emd_42926_half_map_2.map.gz | 45.6 MB 86.1 MB 36.7 MB 84.7 MB 84.6 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-42926 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-42926 | HTTPS FTP |
-Validation report
Summary document | emd_42926_validation.pdf.gz | 1.3 MB | Display | EMDB validaton report |
---|---|---|---|---|
Full document | emd_42926_full_validation.pdf.gz | 1.3 MB | Display | |
Data in XML | emd_42926_validation.xml.gz | 18.2 KB | Display | |
Data in CIF | emd_42926_validation.cif.gz | 23.5 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-42926 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-42926 | HTTPS FTP |
-Related structure data
Related structure data | 8v2qC 8v2rC 8v2sC C: citing same article (ref.) |
---|---|
Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
---|
-Map
File | Download / File: emd_42926.map.gz / Format: CCP4 / Size: 91.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Refined symmetrized sharpened map | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.1925 Å | ||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
|
-Supplemental data
-Mask #1
File | emd_42926_msk_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Mask #2
File | emd_42926_msk_2.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Additional map: Refined map
File | emd_42926_additional_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Refined map | ||||||||||||
Projections & Slices |
| ||||||||||||
Density Histograms |
-Additional map: Refined sharpened map
File | emd_42926_additional_2.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Refined sharpened map | ||||||||||||
Projections & Slices |
| ||||||||||||
Density Histograms |
-Additional map: Refined symmetrized map
File | emd_42926_additional_3.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Refined symmetrized map | ||||||||||||
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: Refined half map B
File | emd_42926_half_map_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Refined half map B | ||||||||||||
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: Refined half map A
File | emd_42926_half_map_2.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Refined half map A | ||||||||||||
Projections & Slices |
| ||||||||||||
Density Histograms |
-Sample components
-Entire : CHMP1B/IST1 copolymer isolated and purified from HeLa cell over e...
Entire | Name: CHMP1B/IST1 copolymer isolated and purified from HeLa cell over expression |
---|---|
Components |
|
-Supramolecule #1: CHMP1B/IST1 copolymer isolated and purified from HeLa cell over e...
Supramolecule | Name: CHMP1B/IST1 copolymer isolated and purified from HeLa cell over expression type: complex / ID: 1 / Parent: 0 / Macromolecule list: all Details: pCAG-Myc-IST1 and pCAG-CHMP1B-FOS expression plasmids were transfected into HeLa cells. CHMP1B/IST1 filaments formed in cells. Cytoplasmic filaments were isolated, extracted, and purified ...Details: pCAG-Myc-IST1 and pCAG-CHMP1B-FOS expression plasmids were transfected into HeLa cells. CHMP1B/IST1 filaments formed in cells. Cytoplasmic filaments were isolated, extracted, and purified for generation of this sample |
---|---|
Source (natural) | Organism: Homo sapiens (human) |
-Supramolecule #2: Charged multivesicular body protein 1B (CHMP1B)
Supramolecule | Name: Charged multivesicular body protein 1B (CHMP1B) / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1 Details: CHMP1B component of the nucleic acid templated helical assembly |
---|---|
Source (natural) | Organism: Homo sapiens (human) / Location in cell: Cytoplasm |
-Supramolecule #3: Increased sodium tolerance 1 (IST1)
Supramolecule | Name: Increased sodium tolerance 1 (IST1) / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2 Details: IST1 component of the nucleic acid templated assembly |
---|---|
Source (natural) | Organism: Homo sapiens (human) / Location in cell: cytoplasm |
-Macromolecule #1: Charged multivesicular body protein 1B (CHMP1B)
Macromolecule | Name: Charged multivesicular body protein 1B (CHMP1B) / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: Homo sapiens (human) |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: MSNMEKHLFN LKFAAKELSR SAKKCDKEEK AEKAKIKKAI QKGNMEVARI HAENAIRQKN QAVNFLRMS ARVDAVAARV QTAVTMGKVT KSMAGVVKSM DATLKTMNLE KISALMDKFE H QFETLDVQ TQQMEDTMSS TTTLTTPQNQ VDMLLQEMAD EAGLDLNMEL ...String: MSNMEKHLFN LKFAAKELSR SAKKCDKEEK AEKAKIKKAI QKGNMEVARI HAENAIRQKN QAVNFLRMS ARVDAVAARV QTAVTMGKVT KSMAGVVKSM DATLKTMNLE KISALMDKFE H QFETLDVQ TQQMEDTMSS TTTLTTPQNQ VDMLLQEMAD EAGLDLNMEL PQGQTGSVGT SV ASAEQDE LSQRLARLRD QV UniProtKB: Charged multivesicular body protein 1b |
-Macromolecule #2: Increased sodium tolerance 1 (IST1)
Macromolecule | Name: Increased sodium tolerance 1 (IST1) / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: Homo sapiens (human) |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: MLGSGFKAER LRVNLRLVIN RLKLLEKKKT ELAQKARKEI ADYLAAGKDE RARIRVEHII REDYLVEAM EILELYCDLL LARFGLIQSM KELDSGLAES VSTLIWAAPR LQSEVAELKI V ADQLCAKY SKEYGKLCRT NQIGTVNDRL MHKLSVEAPP KILVERYLIE ...String: MLGSGFKAER LRVNLRLVIN RLKLLEKKKT ELAQKARKEI ADYLAAGKDE RARIRVEHII REDYLVEAM EILELYCDLL LARFGLIQSM KELDSGLAES VSTLIWAAPR LQSEVAELKI V ADQLCAKY SKEYGKLCRT NQIGTVNDRL MHKLSVEAPP KILVERYLIE IAKNYNVPYE PD SVVMAEA PPGVETDLID VGFTDDVKKG GPGRGGSGGF TAPVGGPDGT VPMPMPMPMP SAN TPFSYP LPKGPSDFNG LPMGTYQAFP NIHPPQIPAT PPSYESVDDI NADKNISSAQ IVGP GPKPE ASAKLPSRPA DNYDNFVLPE LPSVPDTLPT ASAGASTSAS EDIDFDDLSR RFEEL KKKT UniProtKB: IST1 homolog |
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
Processing | helical reconstruction |
Aggregation state | filament |
-Sample preparation
Buffer | pH: 7.4 Component:
Details: PBS | |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Vitrification | Cryogen name: ETHANE / Chamber humidity: 85 % / Chamber temperature: 284.15 K / Instrument: LEICA EM GP / Details: model: GP2 plunge freezer. | |||||||||||||||
Details | Sample purified via sequential differential centrifugation method to isolate filaments from clarified Hela lysates. |
-Electron microscopy
Microscope | TFS KRIOS |
---|---|
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 1 / Number real images: 3260 / Average electron dose: 46.0 e/Å2 Details: Dataset 1 - 1901 micrographs Dataset 2 - 1359 micrographs |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | C2 aperture diameter: 50.0 µm / Calibrated defocus max: 4.0 µm / Calibrated defocus min: 0.1 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 130000 |
Sample stage | Specimen holder model: OTHER / Cooling holder cryogen: NITROGEN |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |