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Yorodumi- EMDB-33141: cryo-EM map of Dot1L and H3K79Nle nucleosome complex (inactive state) -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-33141 | ||||||||||||||||||
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Title | cryo-EM map of Dot1L and H3K79Nle nucleosome complex (inactive state) | ||||||||||||||||||
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Sample |
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Keywords | Dot1L / Nucleosome / H3K79Nle / NUCLEAR PROTEIN | ||||||||||||||||||
Biological species | Homo sapiens (human) | ||||||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.27 Å | ||||||||||||||||||
Authors | Ai HS / Liu AJ / Lou ZY / Liu L | ||||||||||||||||||
Funding support | China, 5 items
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Citation | Journal: Nat Chem Biol / Year: 2022 Title: H2B Lys34 Ubiquitination Induces Nucleosome Distortion to Stimulate Dot1L Activity. Authors: Huasong Ai / Maoshen Sun / Aijun Liu / Zixian Sun / Tingting Liu / Lin Cao / Lujun Liang / Qian Qu / Zichen Li / Zhiheng Deng / Zebin Tong / Guochao Chu / Xiaolin Tian / Haiteng Deng / Suwen ...Authors: Huasong Ai / Maoshen Sun / Aijun Liu / Zixian Sun / Tingting Liu / Lin Cao / Lujun Liang / Qian Qu / Zichen Li / Zhiheng Deng / Zebin Tong / Guochao Chu / Xiaolin Tian / Haiteng Deng / Suwen Zhao / Jia-Bin Li / Zhiyong Lou / Lei Liu / Abstract: Ubiquitination-dependent histone crosstalk plays critical roles in chromatin-associated processes and is highly associated with human diseases. Mechanism studies of the crosstalk have been of the ...Ubiquitination-dependent histone crosstalk plays critical roles in chromatin-associated processes and is highly associated with human diseases. Mechanism studies of the crosstalk have been of the central focus. Here our study on the crosstalk between H2BK34ub and Dot1L-catalyzed H3K79me suggests a novel mechanism of ubiquitination-induced nucleosome distortion to stimulate the activity of an enzyme. We determined the cryo-electron microscopy structures of Dot1L-H2BK34ub nucleosome complex and the H2BK34ub nucleosome alone. The structures reveal that H2BK34ub induces an almost identical orientation and binding pattern of Dot1L on nucleosome as H2BK120ub, which positions Dot1L for the productive conformation through direct ubiquitin-enzyme contacts. However, H2BK34-anchored ubiquitin does not directly interact with Dot1L as occurs in the case of H2BK120ub, but rather induces DNA and histone distortion around the modified site. Our findings establish the structural framework for understanding the H2BK34ub-H3K79me trans-crosstalk and highlight the diversity of mechanisms for histone ubiquitination to activate chromatin-modifying enzymes. | ||||||||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_33141.map.gz | 5.2 MB | EMDB map data format | |
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Header (meta data) | emd-33141-v30.xml emd-33141.xml | 15.3 KB 15.3 KB | Display Display | EMDB header |
Images | emd_33141.png | 47.9 KB | ||
Masks | emd_33141_msk_1.map | 64 MB | Mask map | |
Filedesc metadata | emd-33141.cif.gz | 3.9 KB | ||
Others | emd_33141_additional_1.map.gz emd_33141_half_map_1.map.gz emd_33141_half_map_2.map.gz | 49.5 MB 49.7 MB 49.8 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-33141 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-33141 | HTTPS FTP |
-Validation report
Summary document | emd_33141_validation.pdf.gz | 710.6 KB | Display | EMDB validaton report |
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Full document | emd_33141_full_validation.pdf.gz | 710.1 KB | Display | |
Data in XML | emd_33141_validation.xml.gz | 12.2 KB | Display | |
Data in CIF | emd_33141_validation.cif.gz | 14.4 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-33141 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-33141 | HTTPS FTP |
-Related structure data
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_33141.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.0979 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
File | emd_33141_msk_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Additional map: #1
File | emd_33141_additional_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_33141_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_33141_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Complex of Dot1L(1-416) and H3K79Nle nucleosome (inactive state)
Entire | Name: Complex of Dot1L(1-416) and H3K79Nle nucleosome (inactive state) |
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Components |
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-Supramolecule #1: Complex of Dot1L(1-416) and H3K79Nle nucleosome (inactive state)
Supramolecule | Name: Complex of Dot1L(1-416) and H3K79Nle nucleosome (inactive state) type: complex / ID: 1 / Parent: 0 |
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Source (natural) | Organism: Homo sapiens (human) |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: OTHER |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.27 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 530669 |
Initial angle assignment | Type: ANGULAR RECONSTITUTION |
Final angle assignment | Type: ANGULAR RECONSTITUTION |