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Yorodumi- EMDB-55943: Structure of the H4.V variant nucleosome core particle from Trypa... -
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Open data
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Basic information
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| Title | Structure of the H4.V variant nucleosome core particle from Trypanosoma brucei | |||||||||
Map data | Sharpened map | |||||||||
Sample |
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Keywords | nucleosome / histone / nucleus / DNA BINDING PROTEIN | |||||||||
| Function / homology | Function and homology informationphosphate ion binding / chromosome organization / structural constituent of chromatin / nucleosome / heterochromatin formation / nucleosome assembly / protein heterodimerization activity / DNA binding / nucleoplasm / nucleus Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.99 Å | |||||||||
Authors | Deak G / Wilson MD | |||||||||
| Funding support | United Kingdom, 2 items
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Citation | Journal: Structure / Year: 2026Title: Trypanosome histone variants H3.V and H4.V promote nucleosome plasticity in repressed chromatin. Authors: Gauri Deák / Hayden Burdett / James A Watson / Marcus D Wilson / ![]() Abstract: Histone variants define distinct chromatin states by modulating the biophysical properties of nucleosomes. Variants play a particularly important role in the parasitic protist Trypanosoma brucei, ...Histone variants define distinct chromatin states by modulating the biophysical properties of nucleosomes. Variants play a particularly important role in the parasitic protist Trypanosoma brucei, which has unusual chromatin and lacks a canonical repressive heterochromatin system. Instead, T. brucei utilizes specialized divergent histone variants H3.V and H4.V. However, the biochemical basis of their repressive functions is unknown. Here, we determined the structure of the H3.V-H4.V nucleosome core particle and biochemically characterized variant-containing nucleosomes and nucleosome arrays, probing their unique properties. We discovered that surprisingly for repressive-state nucleosomes, H3.V promotes pronounced DNA splaying, largely via its N-terminal tail region, while retaining overall stability that is comparable to canonical nucleosomes. In contrast, H4.V exhibits near-identical binding to DNA but mediates a slight increase in histone octamer stability. The surface of the H3.V-H4.V nucleosome is altered and provides a differential platform for chromatin-binding proteins, linking the variants to parasite pathogenicity. | |||||||||
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_55943.map.gz | 118 MB | EMDB map data format | |
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| Header (meta data) | emd-55943-v30.xml emd-55943.xml | 29.5 KB 29.5 KB | Display Display | EMDB header |
| FSC (resolution estimation) | emd_55943_fsc.xml | 10.7 KB | Display | FSC data file |
| Images | emd_55943.png | 56.5 KB | ||
| Masks | emd_55943_msk_1.map | 125 MB | Mask map | |
| Filedesc metadata | emd-55943.cif.gz | 6.4 KB | ||
| Others | emd_55943_additional_1.map.gz emd_55943_half_map_1.map.gz emd_55943_half_map_2.map.gz | 62 MB 116.1 MB 116.1 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-55943 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-55943 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9r1dC 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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| Related items in Molecule of the Month |
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Map
| File | Download / File: emd_55943.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | Sharpened map | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 0.7 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Mask #1
| File | emd_55943_msk_1.map | ||||||||||||
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| Density Histograms |
-Additional map: Unsharpened map
| File | emd_55943_additional_1.map | ||||||||||||
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| Annotation | Unsharpened map | ||||||||||||
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| Density Histograms |
-Half map: half map B
| File | emd_55943_half_map_1.map | ||||||||||||
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| Annotation | half map B | ||||||||||||
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| Density Histograms |
-Half map: half map A
| File | emd_55943_half_map_2.map | ||||||||||||
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| Annotation | half map A | ||||||||||||
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| Density Histograms |
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Sample components
-Entire : H4.V variant nucleosome core particle from Trypanosoma brucei rec...
| Entire | Name: H4.V variant nucleosome core particle from Trypanosoma brucei reconstituted with Widom 601 145 bp DNA |
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| Components |
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-Supramolecule #1: H4.V variant nucleosome core particle from Trypanosoma brucei rec...
| Supramolecule | Name: H4.V variant nucleosome core particle from Trypanosoma brucei reconstituted with Widom 601 145 bp DNA type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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| Source (natural) | Organism: ![]() |
| Molecular weight | Theoretical: 89.64 KDa |
-Supramolecule #2: Histone octamer
| Supramolecule | Name: Histone octamer / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#4 |
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| Source (natural) | Organism: ![]() |
-Supramolecule #3: Widom 601 145 bp DNA
| Supramolecule | Name: Widom 601 145 bp DNA / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #5-#6 |
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| Source (natural) | Organism: ![]() |
-Macromolecule #1: T. brucei Histone H3
| Macromolecule | Name: T. brucei Histone H3 / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Recombinant expression | Organism: ![]() |
| Sequence | String: SRTKETARTK KTITSKKSKK ASKGSDAASG VKTAQRRWRP GTVALREIRQ FQRSTDLLLQ KAPFQRLVRE VSGAQKEGLR FQSSAILAAQ EATESYIVSL LADTNRACIH SGRVTIQPKD IHLALCLRGE RA UniProtKB: Histone H3 |
-Macromolecule #2: T. brucei Histone H4.V
| Macromolecule | Name: T. brucei Histone H4.V / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Recombinant expression | Organism: ![]() |
| Sequence | String: AKGKRVGESK GAQKRQKKVL RDNVRGITRG SIRRLARRAG VKRISGVIYD EVRGVLKTFV ESIVRDAGAY TEYSRKKTVT AAHVVFALRK RGKVLYGYD UniProtKB: Histone H4 |
-Macromolecule #3: T. brucei Histone H2A
| Macromolecule | Name: T. brucei Histone H2A / type: protein_or_peptide / ID: 3 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Recombinant expression | Organism: ![]() |
| Sequence | String: ATPKQAVKKA SKGGSSRSVK AGLIFPVGRV GTLLRRGQYA RRIGASGAVY MAAVLEYLTA ELLELSVKAA AQQTKKTKRL TPRTVTLAVR HDDDLGALLR NVTMSRGGVM PSLNKALAKK QKSGKHAKAT PSV UniProtKB: Histone H2A |
-Macromolecule #4: T. brucei Histone H2B
| Macromolecule | Name: T. brucei Histone H2B / type: protein_or_peptide / ID: 4 / Enantiomer: LEVO |
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| Source (natural) | Organism: ![]() |
| Recombinant expression | Organism: ![]() |
| Sequence | String: ATPKSTPAKT RKEAKKTRRQ RKRTWNVYVS RSLRSINSQM SMTSRTMKIV NSFVNDLFER IAAEAATIVR VNRKRTLGAR ELQTAVRLVL PADLAKHAMA EGTKAVSHAS S UniProtKB: Histone H2B |
-Macromolecule #5: Widom 601 145 bp DNA
| Macromolecule | Name: Widom 601 145 bp DNA / type: dna / ID: 5 / Classification: DNA |
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| Source (natural) | Organism: synthetic construct (others) |
| Sequence | String: ATCGATGTAT ATATCTGACA CGTGCCTGGA GACTAGGGAG TAATCCCCTT GGCGGTTAAA ACGCGGGGGA CAGCGCGTAC GTGCGTTTAA GCGGTGCTAG AGCTGTCTAC GACCAATTGA GCGGCCTCGG CACCGGGATT CTGAT |
-Macromolecule #6: Widom 601 145 bp DNA
| Macromolecule | Name: Widom 601 145 bp DNA / type: dna / ID: 6 / Classification: DNA |
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| Source (natural) | Organism: synthetic construct (others) |
| Sequence | String: ATCAGAATCC CGGTGCCGAG GCCGCTCAAT TGGTCGTAGA CAGCTCTAGC ACCGCTTAAA CGCACGTACG CGCTGTCCCC CGCGTTTTAA CCGCCAAGGG GATTACTCCC TAGTCTCCAG GCACCTGTCA GATATATACA TCGAT |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Concentration | 0.07 mg/mL | |||||||||||||||
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| Buffer | pH: 8 Component:
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| Grid | Model: Quantifoil R2/2 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 90 sec. / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 0.038 kPa | |||||||||||||||
| Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV | |||||||||||||||
| Details | Crosslinked with 0.1% glutaraldehyde |
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Electron microscopy
| Microscope | TFS GLACIOS |
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| Specialist optics | Energy filter - Name: TFS Selectris / Energy filter - Slit width: 10 eV |
| Image recording | Film or detector model: TFS FALCON 4i (4k x 4k) / Digitization - Dimensions - Width: 4096 pixel / Digitization - Dimensions - Height: 4096 pixel / Number grids imaged: 1 / Number real images: 10414 / Average exposure time: 3.69 sec. / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | C2 aperture diameter: 20.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.2 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 165000 |
| Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
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Image processing
-Atomic model buiding 1
| Refinement | Overall B value: 113.4 |
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Keywords
Authors
United Kingdom, 2 items
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FIELD EMISSION GUN
