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Yorodumi- PDB-9rl4: Structure of BAF in complex with OCT4-SOX2-bound nucleosome - SHL-6 -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9rl4 | ||||||||||||||||||
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| Title | Structure of BAF in complex with OCT4-SOX2-bound nucleosome - SHL-6 | ||||||||||||||||||
Components |
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Keywords | GENE REGULATION / remodelling / chromatin / transcription | ||||||||||||||||||
| Function / homology | Function and homology informationnegative regulation of myeloid progenitor cell differentiation / glial cell fate commitment / single stranded viral RNA replication via double stranded DNA intermediate / Formation of the posterior neural plate / cell fate commitment involved in formation of primary germ layer / cardiac cell fate determination / POU5F1 (OCT4), SOX2, NANOG repress genes related to differentiation / Formation of the anterior neural plate / Positive Regulation of CDH1 Gene Transcription / endodermal-mesodermal cell signaling ...negative regulation of myeloid progenitor cell differentiation / glial cell fate commitment / single stranded viral RNA replication via double stranded DNA intermediate / Formation of the posterior neural plate / cell fate commitment involved in formation of primary germ layer / cardiac cell fate determination / POU5F1 (OCT4), SOX2, NANOG repress genes related to differentiation / Formation of the anterior neural plate / Positive Regulation of CDH1 Gene Transcription / endodermal-mesodermal cell signaling / regulation of asymmetric cell division / endodermal cell fate specification / positive regulation of glucose mediated signaling pathway / pituitary gland development / blastocyst development / heart induction / bBAF complex / negative regulation of cell cycle G1/S phase transition / POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation / Specification of the neural plate border / neuronal stem cell population maintenance / Specification of primordial germ cells / nBAF complex / Regulation of MITF-M-dependent genes involved in extracellular matrix, focal adhesion and epithelial-to-mesenchymal transition / npBAF complex / brahma complex / positive regulation of norepinephrine uptake / positive regulation of telomere maintenance in response to DNA damage / Transcriptional regulation of pluripotent stem cells / regulation of DNA strand elongation / perichromatin fibrils / negative regulation of androgen receptor signaling pathway / GBAF complex / Transcriptional Regulation by MECP2 / Germ layer formation at gastrulation / positive regulation of transcription of nucleolar large rRNA by RNA polymerase I / eye development / N-acetyltransferase activity / cellular response to cytochalasin B / neural retina development / Formation of the embryonic stem cell BAF (esBAF) complex / EGR2 and SOX10-mediated initiation of Schwann cell myelination / response to growth factor / regulation of transepithelial transport / Formation of the canonical BAF (cBAF) complex / morphogenesis of a polarized epithelium / RSC-type complex / Formation of annular gap junctions / XY body / Formation of the dystrophin-glycoprotein complex (DGC) / Formation of the polybromo-BAF (pBAF) complex / somatic stem cell population maintenance / structural constituent of postsynaptic actin cytoskeleton / Gap junction degradation / GBP-mediated host defense / Formation of neuronal progenitor and neuronal BAF (npBAF and nBAF) / protein localization to adherens junction / Formation of the non-canonical BAF (ncBAF) complex / Cell-extracellular matrix interactions / regulation of G0 to G1 transition / histone H3K14ac reader activity / dense body / Tat protein binding / RNA polymerase I preinitiation complex assembly / Folding of actin by CCT/TriC / cellular response to fatty acid / Regulation of CDH1 Function / Ino80 complex / postsynaptic actin cytoskeleton / host-mediated activation of viral transcription / forebrain development / apical protein localization / Adherens junctions interactions / Prefoldin mediated transfer of substrate to CCT/TriC / microtubule nucleation / RHOF GTPase cycle / adherens junction assembly / regulation of double-strand break repair / SWI/SNF complex / Sensory processing of sound by outer hair cells of the cochlea / nucleosome disassembly / negative regulation of neuron differentiation / ATP-dependent chromatin remodeler activity / miRNA binding / spinal cord development / tight junction / positive regulation of T cell differentiation / regulation of mitotic metaphase/anaphase transition / Sensory processing of sound by inner hair cells of the cochlea / nuclear androgen receptor binding / maintenance of blood-brain barrier / Interaction between L1 and Ankyrins / apical junction complex / inner ear development / regulation of nucleotide-excision repair / nuclear chromosome / positive regulation of stem cell population maintenance / NuA4 histone acetyltransferase complex / regulation of chromosome organization / regulation of norepinephrine uptake Similarity search - Function | ||||||||||||||||||
| Biological species | Homo sapiens (human)![]() synthetic construct (others) | ||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å | ||||||||||||||||||
Authors | Vecchia, L. / Weiss, J. / Cavadini, S. / Kempf, G. / Kater, L. / Pathare, G. / Thoma, N.H. | ||||||||||||||||||
| Funding support | European Union, Switzerland, 5items
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Citation | Journal: Mol Cell / Year: 2026Title: The human BAF chromatin remodeler processes nucleosomes bound by pioneer transcription factors OCT4-SOX2. Authors: Joscha Weiss / Luca Vecchia / David Domjan / Simone Cavadini / Anton Sabantsev / Georg Kempf / Ganesh R Pathare / Klaus Brackmann / Alicia K Michael / Lukas Kater / Eric Hietter-Pfeiffer / ...Authors: Joscha Weiss / Luca Vecchia / David Domjan / Simone Cavadini / Anton Sabantsev / Georg Kempf / Ganesh R Pathare / Klaus Brackmann / Alicia K Michael / Lukas Kater / Eric Hietter-Pfeiffer / Mina Haddawi / Urja P Kuber / Sandra Mühlhäusser / Ralph S Grand / Michael B Stadler / Sebastian Deindl / Nicolas H Thomä / ![]() Abstract: Chromatin remodeling complexes mobilize nucleosomes and promote transcription factor (TF) binding. Using ensemble and single-molecule assays combined with cryo-electron microscopy (cryo-EM), we ...Chromatin remodeling complexes mobilize nucleosomes and promote transcription factor (TF) binding. Using ensemble and single-molecule assays combined with cryo-electron microscopy (cryo-EM), we studied the interaction between pioneer TFs OCT4-SOX2 and the human BRG1/BRM-associated factor (BAF) complex on nucleosomes. BAF engages TF-bound substrates in two orientations, placing OCT4-SOX2 at either the remodeler ENTRY or EXIT site. At the ENTRY site, OCT4-SOX2 initially coexists with BAF without structural interference. However, continued DNA translocation is expected to cause collisions with bound TFs, which can trigger remodeling direction reversals or may induce TF dissociation. To accommodate TFs at the EXIT site, BAF undergoes structural rearrangements, and ensemble assays reveal a nucleosome subpopulation translocating away from TF-binding sites. Moreover, single-molecule experiments show that nucleosome-bound BAF frequently changes remodeling direction, and we identify an ADP-bound remodeler conformation as a potential intermediate. Together, these findings reveal key aspects of the conformational dynamics and remodeling outcomes underlying BAF processing of TF-bound nucleosomes. | ||||||||||||||||||
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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 | 9rl4.cif.gz | 1007.6 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9rl4.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9rl4.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rl/9rl4 ftp://data.pdbj.org/pub/pdb/validation_reports/rl/9rl4 | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 54030MC ![]() 9rmcC ![]() 9rn1C ![]() 9rn2C 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 AEBFCGDHJKLNORV
| #1: Protein | Mass: 15719.445 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human)Gene: HIST1H3A, H3FA, HIST1H3B, H3FL, HIST1H3C, H3FC, HIST1H3D, H3FB, HIST1H3E, H3FD, HIST1H3F, H3FI, HIST1H3G, H3FH, HIST1H3H, H3FK, HIST1H3I, H3FF, HIST1H3J, H3FJ Production host: ![]() #2: Protein | Mass: 11676.703 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human)Gene: HIST1H4A, H4/A, H4FA, HIST1H4B, H4/I, H4FI, HIST1H4C, H4/G, H4FG, HIST1H4D, H4/B, H4FB, HIST1H4E, H4/J, H4FJ, HIST1H4F, H4/C, H4FC, HIST1H4H, H4/H, H4FH, HIST1H4I, H4/M, H4FM, HIST1H4J, H4/E, ...Gene: HIST1H4A, H4/A, H4FA, HIST1H4B, H4/I, H4FI, HIST1H4C, H4/G, H4FG, HIST1H4D, H4/B, H4FB, HIST1H4E, H4/J, H4FJ, HIST1H4F, H4/C, H4FC, HIST1H4H, H4/H, H4FH, HIST1H4I, H4/M, H4FM, HIST1H4J, H4/E, H4FE, HIST1H4K, H4/D, H4FD, HIST1H4L, H4/K, H4FK, HIST2H4A, H4/N, H4F2, H4FN, HIST2H4, HIST2H4B, H4/O, H4FO, HIST4H4 Production host: ![]() #3: Protein | Mass: 14447.825 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: HIST1H2AB, H2AFM, HIST1H2AE, H2AFA / Production host: ![]() #4: Protein | Mass: 14088.336 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: HIST1H2BJ, H2BFR / Production host: ![]() #6: Protein | | Mass: 47509.812 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293 / References: UniProt: O96019#7: Protein | | Mass: 41782.660 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293 / References: UniProt: P60709#8: Protein | | Mass: 242250.312 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293 / References: UniProt: O14497#10: Protein | Mass: 133048.109 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293 / References: UniProt: Q8TAQ2#13: Protein | | Mass: 48554.125 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DPF2, BAF45D, REQ, UBID4 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: Q92785#14: Protein | | Mass: 70735.531 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Homo sapiens (human)Gene: GFP, POU5F1, OCT3, OCT4, OTF3 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P42212, UniProt: Q01860 |
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-Transcription ... , 2 types, 2 molecules IW
| #5: Protein | Mass: 184923.828 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293References: UniProt: P51532, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement |
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| #15: Protein | Mass: 12718.679 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SOX2 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P48431 |
-SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily ... , 3 types, 3 molecules MPQ
| #9: Protein | Mass: 44199.188 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293 / References: UniProt: Q12824 |
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| #11: Protein | Mass: 58311.391 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293 / References: UniProt: Q96GM5 |
| #12: Protein | Mass: 46710.371 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: HEK293 / References: UniProt: Q969G3 |
-DNA chain , 2 types, 2 molecules XY
| #16: DNA chain | Mass: 69816.469 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
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| #17: DNA chain | Mass: 70362.789 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
-Non-polymers , 2 types, 17 molecules 


| #18: Chemical | ChemComp-PTD / #19: Chemical | ChemComp-ZN / | |
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-Details
| Has ligand of interest | N |
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| Has protein modification | Y |
-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
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| Source (natural) |
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| Source (recombinant) | Organism: Trichoplusia ni (cabbage looper) | ||||||||||||||||||||||||||||||
| Buffer solution | pH: 8 | ||||||||||||||||||||||||||||||
| 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: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2500 nm / Nominal defocus min: 500 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | |||||||||||||||||||||
| 3D reconstruction | Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 179373 / Symmetry type: POINT | |||||||||||||||||||||
| Atomic model building | Protocol: FLEXIBLE FIT / Space: REAL |
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Homo sapiens (human)

Switzerland, 5items
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Trichoplusia ni (cabbage looper)
FIELD EMISSION GUN