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Open data
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Basic information
| Entry | Database: PDB / ID: 9cat | ||||||
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| Title | DeltaArp8 INO80 bound to S.c 0/40 nucleosome, INO80 Core Module | ||||||
Components |
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Keywords | DNA BINDING PROTEIN / Chromatin Remodeler / nucleosome | ||||||
| Function / homology | Function and homology informationTTT Hsp90 cochaperone complex / R2TP complex / regulation of TOR signaling / Swr1 complex / Ino80 complex / telomere maintenance via recombination / ATP-dependent chromatin remodeler activity / box C/D snoRNP assembly / regulation of metabolic process / 3'-5' DNA helicase activity ...TTT Hsp90 cochaperone complex / R2TP complex / regulation of TOR signaling / Swr1 complex / Ino80 complex / telomere maintenance via recombination / ATP-dependent chromatin remodeler activity / box C/D snoRNP assembly / regulation of metabolic process / 3'-5' DNA helicase activity / cellular response to stress / NuA4 histone acetyltransferase complex / chromosome, centromeric region / subtelomeric heterochromatin formation / enzyme regulator activity / DNA helicase activity / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / rRNA processing / 5'-3' DNA helicase activity / histone binding / DNA helicase / transcription by RNA polymerase II / chromosome, telomeric region / protein stabilization / chromatin remodeling / DNA repair / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / chromatin / positive regulation of transcription by RNA polymerase II / ATP hydrolysis activity / DNA binding / ATP binding / nucleus / cytoplasm Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.9 Å | ||||||
Authors | Wu, H. / Kaur, U. / Narlikar, G.J. / Cheng, Y.F. | ||||||
| Funding support | United States, 1items
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Citation | Journal: Science / Year: 2025Title: Autoinhibition imposed by a large conformational switch of INO80 regulates nucleosome positioning. Authors: Upneet Kaur / Hao Wu / Yifan Cheng / Geeta J Narlikar / ![]() Abstract: Increasing the flanking DNA from 40 to 80 base pairs (bp) causes ~100-fold faster nucleosome sliding by INO80. A prevalent hypothesis posits that the Arp8 module within INO80 enables a ruler-like ...Increasing the flanking DNA from 40 to 80 base pairs (bp) causes ~100-fold faster nucleosome sliding by INO80. A prevalent hypothesis posits that the Arp8 module within INO80 enables a ruler-like activity. Using cryogenic electron microscopy, we show that on nucleosomes with 40 bp of flanking DNA, the Arp8 module rotates 180° away from the DNA. Deleting the Arp8 module enables rapid sliding irrespective of flanking DNA length. Thus, rather than enabling a ruler-like activity, the Arp8 module acts as a brake on INO80 remodeling when flanking DNA is short. This autoinhibition-based mechanism has broad implications for understanding how primitive nucleosome mobilization enzymes may have evolved into sophisticated remodelers. | ||||||
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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 | 9cat.cif.gz | 790 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9cat.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9cat.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9cat_validation.pdf.gz | 1.8 MB | Display | wwPDB validaton report |
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| Full document | 9cat_full_validation.pdf.gz | 1.8 MB | Display | |
| Data in XML | 9cat_validation.xml.gz | 107.2 KB | Display | |
| Data in CIF | 9cat_validation.cif.gz | 163.6 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ca/9cat ftp://data.pdbj.org/pub/pdb/validation_reports/ca/9cat | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 45403MC ![]() 9c9gC ![]() 9c9sC ![]() 9c9tC ![]() 9c9xC ![]() 9c9zC ![]() 9canC ![]() 9cauC ![]() 9cb7C ![]() 9ccdC 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
-Chromatin-remodeling ... , 2 types, 2 molecules QS
| #1: Protein | Mass: 171693.812 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: P53115, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement |
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| #3: Protein | Mass: 18564.965 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-Protein , 2 types, 2 molecules RZ
| #2: Protein | Mass: 87682.359 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #6: Protein | Mass: 36210.953 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
-RuvB-like protein ... , 2 types, 6 molecules TVXUWY
| #4: Protein | Mass: 50516.941 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #5: Protein | Mass: 50539.367 Da / Num. of mol.: 3 / Fragment: residues 1-460 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Non-polymers , 1 types, 6 molecules 
| #7: Chemical | ChemComp-ADP / |
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-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: CELL / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: DeltaArp8 INO80 bound to S.c 0/40 nucleosome, INO80 Core Module Type: COMPLEX / Entity ID: #1-#6 / Source: NATURAL |
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| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.5 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: OTHER |
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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 / Nominal defocus max: 2000 nm / Nominal defocus min: 1000 nm |
| Image recording | Electron dose: 47.7 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Version: 1.20.1_4487: / Category: model refinement |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
| 3D reconstruction | Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 36091 / Symmetry type: POINT |
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FIELD EMISSION GUN