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Open data
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Basic information
| Entry | Database: PDB / ID: 8kcb | ||||||
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| Title | Complex of DDM1-nucleosome(H2A) complex with DDM1 bound to SHL2 | ||||||
Components |
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Keywords | STRUCTURAL PROTEIN / DDM1 / nucleosome / H2A | ||||||
| Function / homology | Function and homology informationDNA-mediated transformation / retrotransposition / chromocenter / thylakoid / response to water deprivation / plant-type vacuole / plasmodesma / plastid / DNA methylation-dependent constitutive heterochromatin formation / DNA helicase activity ...DNA-mediated transformation / retrotransposition / chromocenter / thylakoid / response to water deprivation / plant-type vacuole / plasmodesma / plastid / DNA methylation-dependent constitutive heterochromatin formation / DNA helicase activity / epigenetic regulation of gene expression / chloroplast / response to bacterium / response to wounding / structural constituent of chromatin / peroxisome / nucleosome / heterochromatin formation / DNA helicase / chromatin remodeling / protein heterodimerization activity / nucleolus / ATP hydrolysis activity / DNA binding / extracellular region / ATP binding / nucleus / plasma membrane / cytosol Similarity search - Function | ||||||
| Biological species | ![]() synthetic construct (others) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.17 Å | ||||||
Authors | Zhang, H. / Zhang, Y. | ||||||
| Funding support | China, 1items
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Citation | Journal: Structure / Year: 2024Title: Mechanism of heterochromatin remodeling revealed by the DDM1 bound nucleosome structures. Authors: Hongwei Zhang / Zhanxi Gu / Yuan Zeng / Yu Zhang / ![]() Abstract: The SWI/SNF2 chromatin remodeling factor decreased DNA methylation 1 (DDM1) is essential for the silencing of transposable elements (TEs) in both euchromatic and heterochromatic regions. Here, we ...The SWI/SNF2 chromatin remodeling factor decreased DNA methylation 1 (DDM1) is essential for the silencing of transposable elements (TEs) in both euchromatic and heterochromatic regions. Here, we determined the cryo-EM structures of DDM1-nucleosome and DDM1-nucleosome complexes at near-atomic resolution in the presence of the ATP analog ADP-BeFx. The structures show that nucleosomal DNA is unwrapped more on the surface of the histone octamer containing histone H2A than that containing histone H2A.W. DDM1 embraces one DNA gyre of the nucleosome and interacts with the N-terminal tails of histone H4. Although we did not observe DDM1-H2A.W interactions in our structures, the results of the pull-down experiments suggest a direct interaction between DDM1 and the core region of histone H2A.W. Our work provides mechanistic insights into the heterochromatin remodeling process driven by DDM1 in plants. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 8kcb.cif.gz | 379.7 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb8kcb.ent.gz | 286.1 KB | Display | PDB format |
| PDBx/mmJSON format | 8kcb.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8kcb_validation.pdf.gz | 1.6 MB | Display | wwPDB validaton report |
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| Full document | 8kcb_full_validation.pdf.gz | 1.6 MB | Display | |
| Data in XML | 8kcb_validation.xml.gz | 51.7 KB | Display | |
| Data in CIF | 8kcb_validation.cif.gz | 78.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kc/8kcb ftp://data.pdbj.org/pub/pdb/validation_reports/kc/8kcb | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 37098MC ![]() 8kccC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-Protein , 5 types, 9 molecules DCFEHGABK
| #1: Protein | Mass: 15767.544 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Protein | Mass: 15300.968 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: HTR2, At1g09200, T12M4.9, HTR3, At3g27360, K1G2.8, HTR13, At5g10390, F12B17_260, HTR9, At5g10400, F12B17_250, HTR1, At5g65360, MNA5.9 Production host: ![]() #3: Protein | Mass: 11436.467 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: At1g07660, F24B9.25, At1g07820, F24B9.8, At2g28740, F8N16.2, T11P11.4, At3g45930, F16L2_140, At3g46320, F18L15.40, At3g53730, F5K20_30, At5g59690, MTH12.10, At5g59970, MMN10.22 Production host: ![]() #4: Protein | Mass: 13680.854 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #7: Protein | | Mass: 86757.758 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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-DNA chain , 2 types, 2 molecules IJ
| #5: DNA chain | Mass: 52199.215 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
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| #6: DNA chain | Mass: 52764.609 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
-Non-polymers , 2 types, 2 molecules 


| #8: Chemical | ChemComp-BEF / |
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| #9: Chemical | ChemComp-ADP / |
-Details
| Has ligand of interest | N |
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-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Complex of DDM1-nucleosome(H2A.W) complex with DDM1 bound to SHL2 Type: COMPLEX / Entity ID: #1-#7 / Source: MULTIPLE SOURCES |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: ![]() |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 7.5 |
| Specimen | Conc.: 2 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3 |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TITAN KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1000 nm |
| Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Version: 1.20.1_4487: / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING ONLY | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.17 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 239089 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Cross valid method: NONE | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi






China, 1items
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FIELD EMISSION GUN