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Open data
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Basic information
| Entry | Database: PDB / ID: 7ksr | ||||||
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| Title | PRC2:EZH1_A from a dimeric PRC2 bound to a nucleosome | ||||||
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Keywords | GENE REGULATION/Transferase / Chromatin / methyltransferase / nucleosome-modifying complex / GENE REGULATION / GENE REGULATION-Transferase complex | ||||||
| Function / homology | Function and homology information[histone H3]-lysine27 N-trimethyltransferase / CAF-1 complex / histone H3K27 trimethyltransferase activity / random inactivation of X chromosome / regulation of adaxial/abaxial pattern formation / histone H3K27 methyltransferase activity / sex chromatin / NURF complex / facultative heterochromatin formation / NuRD complex ...[histone H3]-lysine27 N-trimethyltransferase / CAF-1 complex / histone H3K27 trimethyltransferase activity / random inactivation of X chromosome / regulation of adaxial/abaxial pattern formation / histone H3K27 methyltransferase activity / sex chromatin / NURF complex / facultative heterochromatin formation / NuRD complex / regulation of cell fate specification / negative regulation of stem cell population maintenance / genomic imprinting / DNA replication-dependent chromatin assembly / Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1 / ESC/E(Z) complex / regulation of stem cell differentiation / RSC-type complex / protein-lysine N-methyltransferase activity / Polo-like kinase mediated events / chromatin silencing complex / histone H3K9me2/3 reader activity / Transcription of E2F targets under negative control by DREAM complex / pronucleus / spinal cord development / ATPase complex / lncRNA binding / G1/S-Specific Transcription / Sin3-type complex / Transcriptional Regulation by E2F6 / : / positive regulation of stem cell population maintenance / oligodendrocyte differentiation / histone deacetylase complex / RNA Polymerase I Transcription Initiation / G0 and Early G1 / negative regulation of cell differentiation / anatomical structure morphogenesis / subtelomeric heterochromatin formation / heterochromatin / Cyclin E associated events during G1/S transition / Transcriptional regulation of brown and beige adipocyte differentiation by EBF2 / Cyclin A:Cdk2-associated events at S phase entry / nucleosome binding / Regulation of TP53 Activity through Acetylation / Deposition of new CENPA-containing nucleosomes at the centromere / negative regulation of cell migration / SUMOylation of chromatin organization proteins / cellular response to leukemia inhibitory factor / Regulation of PTEN gene transcription / transcription corepressor binding / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / PRC2 methylates histones and DNA / Regulation of endogenous retroelements by KRAB-ZFP proteins / Defective pyroptosis / hippocampus development / HDACs deacetylate histones / Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) / enzyme activator activity / promoter-specific chromatin binding / molecular condensate scaffold activity / negative regulation of transforming growth factor beta receptor signaling pathway / protein-DNA complex / brain development / chromatin DNA binding / PKMTs methylate histone lysines / histone deacetylase binding / Activation of anterior HOX genes in hindbrain development during early embryogenesis / HCMV Early Events / transcription corepressor activity / heterochromatin formation / nucleosome assembly / histone binding / Oxidative Stress Induced Senescence / methylation / Potential therapeutics for SARS / chromosome, telomeric region / DNA replication / cell population proliferation / nuclear body / RNA polymerase II cis-regulatory region sequence-specific DNA binding / chromatin remodeling / ribonucleoprotein complex / negative regulation of cell population proliferation / DNA repair / negative regulation of DNA-templated transcription / positive regulation of cell population proliferation / chromatin binding / regulation of DNA-templated transcription / chromatin / positive regulation of DNA-templated transcription / nucleolus / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / protein-containing complex / zinc ion binding / nucleoplasm / identical protein binding / nucleus / cytosol Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.1 Å | ||||||
Authors | Grau, D.J. / Armache, K.J. | ||||||
| Funding support | United States, 1items
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Citation | Journal: Nat Commun / Year: 2021Title: Structures of monomeric and dimeric PRC2:EZH1 reveal flexible modules involved in chromatin compaction. Authors: Daniel Grau / Yixiao Zhang / Chul-Hwan Lee / Marco Valencia-Sánchez / Jenny Zhang / Miao Wang / Marlene Holder / Vladimir Svetlov / Dongyan Tan / Evgeny Nudler / Danny Reinberg / Thomas ...Authors: Daniel Grau / Yixiao Zhang / Chul-Hwan Lee / Marco Valencia-Sánchez / Jenny Zhang / Miao Wang / Marlene Holder / Vladimir Svetlov / Dongyan Tan / Evgeny Nudler / Danny Reinberg / Thomas Walz / Karim-Jean Armache / ![]() Abstract: Polycomb repressive complex 2 (PRC2) is a histone methyltransferase critical for maintaining gene silencing during eukaryotic development. In mammals, PRC2 activity is regulated in part by the ...Polycomb repressive complex 2 (PRC2) is a histone methyltransferase critical for maintaining gene silencing during eukaryotic development. In mammals, PRC2 activity is regulated in part by the selective incorporation of one of two paralogs of the catalytic subunit, EZH1 or EZH2. Each of these enzymes has specialized biological functions that may be partially explained by differences in the multivalent interactions they mediate with chromatin. Here, we present two cryo-EM structures of PRC2:EZH1, one as a monomer and a second one as a dimer bound to a nucleosome. When bound to nucleosome substrate, the PRC2:EZH1 dimer undergoes a dramatic conformational change. We demonstrate that mutation of a divergent EZH1/2 loop abrogates the nucleosome-binding and methyltransferase activities of PRC2:EZH1. Finally, we show that PRC2:EZH1 dimers are more effective than monomers at promoting chromatin compaction, and the divergent EZH1/2 loop is essential for this function, thereby tying together the methyltransferase, nucleosome-binding, and chromatin-compaction activities of PRC2:EZH1. We speculate that the conformational flexibility and the ability to dimerize enable PRC2 to act on the varied chromatin substrates it encounters in the cell. | ||||||
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Structure visualization
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 7ksr.cif.gz | 294.9 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb7ksr.ent.gz | 222.7 KB | Display | PDB format |
| PDBx/mmJSON format | 7ksr.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 7ksr_validation.pdf.gz | 877.2 KB | Display | wwPDB validaton report |
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| Full document | 7ksr_full_validation.pdf.gz | 881.2 KB | Display | |
| Data in XML | 7ksr_validation.xml.gz | 42 KB | Display | |
| Data in CIF | 7ksr_validation.cif.gz | 64.1 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ks/7ksr ftp://data.pdbj.org/pub/pdb/validation_reports/ks/7ksr | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 23024MC ![]() 7ksoC ![]() 7ktpC ![]() 7ktqC C: citing same article ( M: map data used to model this data |
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| Similar structure data |
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 85394.141 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: EZH1, KIAA0388 / Production host: ![]() References: UniProt: Q92800, [histone H3]-lysine27 N-trimethyltransferase | ||
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| #2: Protein | Mass: 47709.527 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: RBBP4, RBAP48 / Production host: ![]() | ||
| #3: Protein | Mass: 83181.922 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SUZ12, CHET9, JJAZ1, KIAA0160 / Production host: ![]() | ||
| #4: Protein | Mass: 50267.691 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: EED / Production host: ![]() | ||
| #5: Chemical | ChemComp-ZN / Has ligand of interest | N | |
-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: PRC2:EZH1_A from a PRC2:EZH1 dimer bound to a nucleosome Type: COMPLEX / Entity ID: #1-#4 / Source: RECOMBINANT | |||||||||||||||||||||||||
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| Molecular weight | Value: .266 MDa / Experimental value: NO | |||||||||||||||||||||||||
| Source (natural) | Organism: Homo sapiens (human) | |||||||||||||||||||||||||
| Source (recombinant) | Organism: ![]() | |||||||||||||||||||||||||
| Buffer solution | pH: 7.9 | |||||||||||||||||||||||||
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| Specimen | Conc.: 0.12 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | |||||||||||||||||||||||||
| 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: SPOT SCAN |
| Electron lens | Mode: BRIGHT FIELD |
| Image recording | Electron dose: 56.7 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| EM software | Name: cryoSPARC / Category: CTF correction |
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| CTF correction | Details: Patch CTF correction / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
| Particle selection | Num. of particles selected: 3410000 / Details: Template based picking |
| 3D reconstruction | Resolution: 4.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 18151 / Symmetry type: POINT |
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About Yorodumi




Homo sapiens (human)
United States, 1items
Citation
UCSF Chimera
















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