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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 | |||||||||||||||
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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 / Formation of the embryonic stem cell BAF (esBAF) complex / bBAF complex / cellular response to cytochalasin B / neural retina development ...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 / Formation of the embryonic stem cell BAF (esBAF) complex / bBAF complex / cellular response to cytochalasin B / neural retina development / npBAF complex / brahma complex / nBAF complex / negative regulation of androgen receptor signaling pathway / Formation of the canonical BAF (cBAF) complex / blastocyst hatching / regulation of transepithelial transport / EGR2 and SOX10-mediated initiation of Schwann cell myelination / hepatocyte differentiation / N-acetyltransferase activity / Formation of neuronal progenitor and neuronal BAF (npBAF and nBAF) / coronary artery morphogenesis / Formation of the polybromo-BAF (pBAF) complex / morphogenesis of a polarized epithelium / Formation of annular gap junctions / Formation of the dystrophin-glycoprotein complex (DGC) / structural constituent of postsynaptic actin cytoskeleton / Formation of the non-canonical BAF (ncBAF) complex / Gap junction degradation / Folding of actin by CCT/TriC / GBAF complex / Cell-extracellular matrix interactions / regulation of G0 to G1 transition / protein localization to adherens junction / dense body / Tat protein binding / nucleosome array spacer activity / histone H3K14ac reader activity / RNA polymerase I preinitiation complex assembly / postsynaptic actin cytoskeleton / Ino80 complex / Prefoldin mediated transfer of substrate to CCT/TriC / Regulation of CDH1 Function / RSC-type complex / blastocyst formation / cellular response to fatty acid / XY body / host-mediated activation of viral transcription / regulation of double-strand break repair / regulation of nucleotide-excision repair / Adherens junctions interactions / germ cell nucleus / RHOF GTPase cycle / adherens junction assembly / nucleosome disassembly / apical protein localization / ATP-dependent chromatin remodeler activity / Sensory processing of sound by outer hair cells of the cochlea / Interaction between L1 and Ankyrins / regulation of mitotic metaphase/anaphase transition / tight junction / SWI/SNF complex / Sensory processing of sound by inner hair cells of the cochlea / positive regulation of T cell differentiation / nuclear androgen receptor binding / apical junction complex / negative regulation of G1/S transition of mitotic cell cycle / positive regulation of double-strand break repair / histone acetyltransferase activity / nuclear chromosome / spinal cord development / regulation of chromosome organization / regulation of norepinephrine uptake / transporter regulator activity / maintenance of blood-brain barrier / homeostatic process / positive regulation of stem cell population maintenance / NuA4 histone acetyltransferase complex / establishment or maintenance of cell polarity / RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known / Recycling pathway of L1 / Regulation of MITF-M-dependent genes involved in pigmentation / cortical cytoskeleton / regulation of DNA replication / nitric-oxide synthase binding / regulation of embryonic development / regulation of G1/S transition of mitotic cell cycle / brush border / EPH-ephrin mediated repulsion of cells / negative regulation of cell differentiation / RHO GTPases Activate WASPs and WAVEs / cardiac muscle cell proliferation / embryonic organ development / regulation of synaptic vesicle endocytosis / positive regulation of myoblast differentiation / kinesin binding / positive regulation of signal transduction by p53 class mediator / ATP-dependent activity, acting on DNA / regulation of DNA repair / positive regulation of Wnt signaling pathway 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. | |||||||||||||||
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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
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/vd/7vdv ftp://data.pdbj.org/pub/pdb/validation_reports/vd/7vdv | HTTPS FTP |
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-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