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Yorodumi- PDB-7vdv: The overall structure of human chromatin remodeling PBAF-nucleoso... -
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Basic information
| Entry | Database: PDB / ID: 7vdv | |||||||||||||||
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| Title | The overall structure of human chromatin remodeling PBAF-nucleosome complex | |||||||||||||||
Components |
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Keywords | DNA BINDING PROTEIN / complex | |||||||||||||||
| Function / homology | Function and homology informationsingle stranded viral RNA replication via double stranded DNA intermediate / positive regulation of glucose mediated signaling pathway / regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / positive regulation of norepinephrine uptake / positive regulation of transcription of nucleolar large rRNA by RNA polymerase I / cellular response to cytochalasin B / bBAF complex / neural retina development / npBAF complex ...single stranded viral RNA replication via double stranded DNA intermediate / positive regulation of glucose mediated signaling pathway / regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / positive regulation of norepinephrine uptake / positive regulation of transcription of nucleolar large rRNA by RNA polymerase I / cellular response to cytochalasin B / bBAF complex / neural retina development / npBAF complex / nBAF complex / histone H3K14ac reader activity / brahma complex / negative regulation of androgen receptor signaling pathway / N-acetyltransferase activity / blastocyst hatching / regulation of transepithelial transport / EGR2 and SOX10-mediated initiation of Schwann cell myelination / nucleosome array spacer activity / hepatocyte differentiation / Formation of annular gap junctions / morphogenesis of a polarized epithelium / Formation of the dystrophin-glycoprotein complex (DGC) / structural constituent of postsynaptic actin cytoskeleton / Gap junction degradation / GBAF complex / coronary artery morphogenesis / Folding of actin by CCT/TriC / regulation of G0 to G1 transition / protein localization to adherens junction / Cell-extracellular matrix interactions / dense body / postsynaptic actin cytoskeleton / Tat protein binding / Ino80 complex / XY body / RNA polymerase I preinitiation complex assembly / blastocyst formation / Prefoldin mediated transfer of substrate to CCT/TriC / RSC-type complex / ATP-dependent chromatin remodeler activity / regulation of double-strand break repair / cellular response to fatty acid / regulation of nucleotide-excision repair / host-mediated activation of viral transcription / Adherens junctions interactions / RHOF GTPase cycle / adherens junction assembly / nucleosome disassembly / apical protein localization / germ cell nucleus / Sensory processing of sound by outer hair cells of the cochlea / Interaction between L1 and Ankyrins / tight junction / SWI/SNF complex / regulation of mitotic metaphase/anaphase transition / Sensory processing of sound by inner hair cells of the cochlea / positive regulation of T cell differentiation / nuclear androgen receptor binding / apical junction complex / nuclear chromosome / negative regulation of G1/S transition of mitotic cell cycle / homeostatic process / positive regulation of double-strand break repair / regulation of norepinephrine uptake / spinal cord development / transporter regulator activity / maintenance of blood-brain barrier / regulation of chromosome organization / nitric-oxide synthase binding / cortical cytoskeleton / NuA4 histone acetyltransferase complex / RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known / establishment or maintenance of cell polarity / positive regulation of stem cell population maintenance / Regulation of MITF-M-dependent genes involved in pigmentation / Recycling pathway of L1 / regulation of DNA replication / brush border / regulation of G1/S transition of mitotic cell cycle / regulation of embryonic development / positive regulation of signal transduction by p53 class mediator / EPH-ephrin mediated repulsion of cells / kinesin binding / negative regulation of cell differentiation / RHO GTPases Activate WASPs and WAVEs / positive regulation of Wnt signaling pathway / regulation of synaptic vesicle endocytosis / cardiac muscle cell proliferation / embryonic organ development / ATP-dependent activity, acting on DNA / positive regulation of myoblast differentiation / RHO GTPases activate IQGAPs / heart morphogenesis / histone acetyltransferase activity / regulation of DNA repair / regulation of protein localization to plasma membrane / positive regulation of double-strand break repair via homologous recombination / Chromatin modifying enzymes / Regulation of TP53 Activity through Acetylation Similarity search - Function | |||||||||||||||
| Biological species | Homo sapiens (human)unidentified (others) synthetic construct (others) | |||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å | |||||||||||||||
Authors | Chen, Z.C. / Chen, K.J. / Yuan, J.J. | |||||||||||||||
| Funding support | China, 1items
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Citation | Journal: Nature / Year: 2022Title: Structure of human chromatin-remodelling PBAF complex bound to a nucleosome. Authors: Junjie Yuan / Kangjing Chen / Wenbo Zhang / Zhucheng Chen / ![]() Abstract: DNA wraps around the histone octamer to form nucleosomes, the repeating unit of chromatin, which create barriers for accessing genetic information. Snf2-like chromatin remodellers couple the energy ...DNA wraps around the histone octamer to form nucleosomes, the repeating unit of chromatin, which create barriers for accessing genetic information. Snf2-like chromatin remodellers couple the energy of ATP binding and hydrolysis to reposition and recompose the nucleosome, and have vital roles in various chromatin-based transactions. Here we report the cryo-electron microscopy structure of the 12-subunit human chromatin-remodelling polybromo-associated BRG1-associated factor (PBAF) complex bound to the nucleosome. The motor subunit SMARCA4 engages the nucleosome in the active conformation, which reveals clustering of multiple disease-associated mutations at the interfaces that are essential for chromatin-remodelling activity. SMARCA4 recognizes the H2A-H2B acidic pocket of the nucleosome through three arginine anchors of the Snf2 ATP coupling (SnAc) domain. PBAF shows notable functional modularity, and most of the auxiliary subunits are interwoven into three lobe-like submodules for nucleosome recognition. The PBAF-specific auxiliary subunit ARID2 acts as the structural core for assembly of the DNA-binding lobe, whereas PBRM1, PHF10 and BRD7 are collectively incorporated into the lobe for histone tail binding. Together, our findings provide mechanistic insights into nucleosome recognition by PBAF and a structural basis for understanding SMARCA4-related human diseases. | |||||||||||||||
| History |
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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 | 7vdv.cif.gz | 1 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb7vdv.ent.gz | 752.6 KB | Display | PDB format |
| PDBx/mmJSON format | 7vdv.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 7vdv_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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| Full document | 7vdv_full_validation.pdf.gz | 1.2 MB | Display | |
| Data in XML | 7vdv_validation.xml.gz | 128 KB | Display | |
| Data in CIF | 7vdv_validation.cif.gz | 203.6 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/vd/7vdv ftp://data.pdbj.org/pub/pdb/validation_reports/vd/7vdv | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 31926MC ![]() 7vdtC 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 , 10 types, 15 molecules BFCGDHEKNPQRWXa
| #1: Protein | Mass: 11394.426 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #2: Protein | Mass: 14109.436 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #3: Protein | Mass: 13965.265 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #4: Protein | Mass: 15435.126 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #8: Protein | | Mass: 47509.812 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ARP4 / Production host: Homo sapiens (human) / References: UniProt: O96019#9: Protein | | Mass: 41782.660 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ACTB / Production host: Homo sapiens (human) / References: UniProt: P60709#10: Protein | | Mass: 97547.102 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ARID2 / Production host: Homo sapiens (human) / References: UniProt: Q68CP9#11: Protein | | Mass: 58254.164 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PHF10 / Production host: Homo sapiens (human) / References: UniProt: Q8WUB8#15: Protein | Mass: 133048.109 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SMARCC2 / Production host: Homo sapiens (human) / References: UniProt: Q8TAQ2#18: Protein | | Mass: 116762.430 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PBRM1, BAF180, PB1 / Production host: Homo sapiens (human) / References: UniProt: Q86U86 |
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-DNA chain , 2 types, 2 molecules IJ
| #5: DNA chain | Mass: 63679.574 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
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| #6: DNA chain | Mass: 64145.816 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
-Isoform 2 of ... , 2 types, 2 molecules AT
| #7: Protein | Mass: 169597.938 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SMARCA4 / Production host: Homo sapiens (human)References: UniProt: P51532, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement |
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| #12: Protein | Mass: 74385.812 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: BRD7 / Production host: Homo sapiens (human) / References: UniProt: Q9NPI1 |
-Protein/peptide , 2 types, 2 molecules UM
| #13: Protein/peptide | Mass: 613.749 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) unidentified (others) / Production host: Homo sapiens (human) |
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| #19: Protein/peptide | Mass: 1379.692 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) unidentified (others) / Production host: Homo sapiens (human) |
-SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily ... , 3 types, 3 molecules VYZ
| #14: Protein | Mass: 44199.188 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SMARCB1 / Production host: Homo sapiens (human) / References: UniProt: Q12824 |
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| #16: Protein | Mass: 60127.332 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SMARCD1 / Production host: Homo sapiens (human) / References: UniProt: Q96GM5 |
| #17: Protein | Mass: 46710.371 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SMARCE1 / Production host: Homo sapiens (human) / References: UniProt: Q969G3 |
-Non-polymers , 3 types, 3 molecules 




| #20: Chemical | ChemComp-BEF / |
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| #21: Chemical | ChemComp-MG / |
| #22: Chemical | ChemComp-ADP / |
-Details
| Has ligand of interest | Y |
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| Has protein modification | 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: The motor-nucleosome module of human chromatin remodeling PBAF-nucleosome complex Type: COMPLEX / Entity ID: #1-#19 / Source: MULTIPLE SOURCES |
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| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.5 |
| Specimen | 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: OTHER |
| Electron lens | Mode: BRIGHT FIELD |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| CTF correction | Type: NONE |
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| 3D reconstruction | Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 137659 / Symmetry type: POINT |
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Homo sapiens (human)
China, 1items
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FIELD EMISSION GUN