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Yorodumi- PDB-9nfw: Human SRCAP-CFDP1-nucleosome complex in the activated state of th... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9nfw | |||||||||||||||
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| Title | Human SRCAP-CFDP1-nucleosome complex in the activated state of the H2A.Z histone exchange reaction (composite structure) | |||||||||||||||
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Keywords | GENE REGULATION / Chromatin Remodeler / Snf2 family ATPase / H2A.Z | |||||||||||||||
| Function / homology | Function and homology informationpositive regulation of lymphoid progenitor cell differentiation / hematopoietic stem cell homeostasis / intestinal stem cell homeostasis / promoter-enhancer loop anchoring activity / telomerase RNA localization to Cajal body / muscle cell differentiation / positive regulation of telomere maintenance in response to DNA damage / regulation of DNA strand elongation / histone chaperone activity / R2TP complex ...positive regulation of lymphoid progenitor cell differentiation / hematopoietic stem cell homeostasis / intestinal stem cell homeostasis / promoter-enhancer loop anchoring activity / telomerase RNA localization to Cajal body / muscle cell differentiation / positive regulation of telomere maintenance in response to DNA damage / regulation of DNA strand elongation / histone chaperone activity / R2TP complex / dynein axonemal particle / RPAP3/R2TP/prefoldin-like complex / Swr1 complex / heart process / establishment of protein localization to chromatin / Ino80 complex / negative regulation of transcription by RNA polymerase I / regulation of double-strand break repair / box C/D snoRNP assembly / ATP-dependent chromatin remodeler activity / nucleolus organization / NuA4 histone acetyltransferase complex / regulation of chromosome organization / positive regulation of transcription by RNA polymerase I / regulation of DNA replication / TFIID-class transcription factor complex binding / positive regulation of DNA damage response, signal transduction by p53 class mediator / MLL1 complex / Telomere Extension By Telomerase / positive regulation of transcription initiation by RNA polymerase II / protein folding chaperone complex / calcium ion homeostasis / cAMP/PKA signal transduction / RNA polymerase II core promoter sequence-specific DNA binding / positive regulation of double-strand break repair via homologous recombination / nucleosome binding / telomere maintenance / regulation of embryonic development / Deposition of new CENPA-containing nucleosomes at the centromere / TBP-class protein binding / transcription initiation-coupled chromatin remodeling / negative regulation of canonical Wnt signaling pathway / cellular response to estradiol stimulus / euchromatin / ADP binding / chromatin DNA binding / beta-catenin binding / Formation of the beta-catenin:TCF transactivating complex / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / histone deacetylase binding / DNA Damage Recognition in GG-NER / nuclear matrix / nucleosomal DNA binding / innate immune response in mucosa / positive regulation of canonical Wnt signaling pathway / cellular response to UV / transcription corepressor activity / histone binding / structural constituent of chromatin / nucleosome assembly / UCH proteinases / nucleosome / protein folding / HATs acetylate histones / ATPase binding / DNA recombination / chromatin organization / ciliary basal body / antimicrobial humoral immune response mediated by antimicrobial peptide / spermatogenesis / heterochromatin formation / antibacterial humoral response / DNA helicase / cytoskeleton / regulation of cell cycle / nuclear body / regulation of apoptotic process / DNA helicase activity / transcription coactivator activity / nuclear speck / chromatin remodeling / protein stabilization / ribonucleoprotein complex / Ub-specific processing proteases / RNA polymerase II cis-regulatory region sequence-specific DNA binding / cadherin binding / DNA repair / protein heterodimerization activity / chromosome / centrosome / regulation of transcription by RNA polymerase II / regulation of DNA-templated transcription / nucleolus / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / perinuclear region of cytoplasm / positive regulation of transcription by RNA polymerase II / protein homodimerization activity / ATP hydrolysis activity / protein-containing complex Similarity search - Function | |||||||||||||||
| Biological species | Homo sapiens (human)synthetic construct (others) | |||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.8 Å | |||||||||||||||
Authors | Louder, R.K. / Park, G. | |||||||||||||||
| Funding support | United States, 1items
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Citation | Journal: Sci Adv / Year: 2026Title: Structural mechanism of histone H2A.Z exchange by human SRCAP-CFDP1 holoenzyme. Authors: Giho Park / Carl Wu / Robert K Louder / ![]() Abstract: The conserved yeast SWR1 and human SRCAP chromatin remodeling complexes catalyze exchange of nucleosomal histone H2A for H2A.Z, but the underlying mechanism has remained obscure. Here, we show that ...The conserved yeast SWR1 and human SRCAP chromatin remodeling complexes catalyze exchange of nucleosomal histone H2A for H2A.Z, but the underlying mechanism has remained obscure. Here, we show that histone exchange by SRCAP requires the transient activator CFDP1 and resolve nine cryo-electron microscopy structures of the SRCAP-CFDP1 holoenzyme that define the stepwise exchange mechanism. CFDP1 recognizes the conformation of the fully engaged SRCAP-nucleosome complex through interactions with multiple subunits-including direct contact with the ATPase domain-and induces conformational transitions that drive extensive DNA unwrapping, eviction of the H2A-H2B dimer, and insertion of the H2A.Z-H2B dimer, all without necessarily requiring hydrolysis of bound ATP. Collectively, these findings provide unprecedented insight into the mechanism of activator- and nucleotide-driven histone exchange from nucleosomal H2A to H2A.Z. | |||||||||||||||
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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 | 9nfw.cif.gz | 1.2 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9nfw.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9nfw.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nf/9nfw ftp://data.pdbj.org/pub/pdb/validation_reports/nf/9nfw | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 49375MC ![]() 9ca7C ![]() 9ca8C ![]() 9ca9C ![]() 9caaC ![]() 9nfvC ![]() 9nfxC ![]() 9nfyC ![]() 9nfzC ![]() 9ng0C ![]() 9pgcC ![]() 9pgdC ![]() 9y3dC ![]() 9y3eC ![]() 9y3fC ![]() 9y3gC ![]() 9y3hC ![]() 9zlaC 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 , 11 types, 19 molecules ABCDEGIFHJPQSRTUWVX
| #1: Protein | Mass: 343915.250 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SRCAP, KIAA0309 / Production host: ![]() References: UniProt: Q6ZRS2, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement | ||||||||||||
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| #2: Protein | Mass: 40658.363 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: K-562 / Organ: BLOOD / Tissue: BONE MARROW / References: UniProt: Q15906 | ||||||||||||
| #3: Protein | Mass: 45857.902 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: K-562 / Organ: BLOOD / Tissue: BONE MARROW / References: UniProt: Q9GZN1 | ||||||||||||
| #4: Protein | Mass: 17567.023 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: K-562 / Organ: BLOOD / Tissue: BONE MARROW / References: UniProt: O43257 | ||||||||||||
| #5: Protein | Mass: 50296.914 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: K-562 / Organ: BLOOD / Tissue: BONE MARROW / References: UniProt: Q9Y265, DNA helicase#6: Protein | Mass: 51222.465 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Cell line: K-562 / Organ: BLOOD / Tissue: BONE MARROW / References: UniProt: Q9Y230, DNA helicase#7: Protein | | Mass: 33646.902 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CFDP1, BCNT, CENP-29 / Production host: ![]() #8: Protein | Mass: 13907.163 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #9: Protein | Mass: 13848.097 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #10: Protein | Mass: 15303.930 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #11: Protein | Mass: 11263.231 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
-DNA chain , 2 types, 2 molecules YZ
| #12: DNA chain | Mass: 87851.664 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
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| #13: DNA chain | Mass: 88190.930 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
-Non-polymers , 4 types, 15 molecules 






| #14: Chemical | | #15: Chemical | ChemComp-MG / #16: Chemical | #17: Chemical | ChemComp-ADP / |
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-Details
| Has ligand of interest | N |
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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
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| Molecular weight |
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| Source (natural) | Cellular location: NUCLEOPLASM / Ncbi tax-ID: 9606 / Organ: BLOOD / Organelle: NUCLEUS / Organism:
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| Buffer solution | pH: 7.6 | |||||||||||||||||||||
| 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: 1600 nm / Nominal defocus min: 800 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Version: 1.21_5207 / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 37606 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||
| Displacement parameters | Biso mean: 109.09 Å2 | ||||||||||||||||||||||||
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About Yorodumi



Homo sapiens (human)
United States, 1items
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FIELD EMISSION GUN