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Open data
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Basic information
| Entry | Database: PDB / ID: 6v8o | |||||||||||||||||||||||||||||||||||||||||||||
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| Title | RSC core | |||||||||||||||||||||||||||||||||||||||||||||
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Keywords | GENE REGULATION / Chromatin remodeler / RSC | |||||||||||||||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationregulation of sporulation resulting in formation of a cellular spore / : / regulation of nuclear cell cycle DNA replication / plasmid maintenance / DNA translocase activity / nucleosome array spacer activity / RSC-type complex / ATP-dependent chromatin remodeler activity / UV-damage excision repair / nucleosome disassembly ...regulation of sporulation resulting in formation of a cellular spore / : / regulation of nuclear cell cycle DNA replication / plasmid maintenance / DNA translocase activity / nucleosome array spacer activity / RSC-type complex / ATP-dependent chromatin remodeler activity / UV-damage excision repair / nucleosome disassembly / SWI/SNF complex / sister chromatid cohesion / sporulation resulting in formation of a cellular spore / nuclear chromosome / rRNA transcription / histone H4 reader activity / chromosome, centromeric region / nucleosome binding / : / cytoskeleton organization / meiotic cell cycle / transcription coregulator activity / chromosome segregation / transcription elongation by RNA polymerase II / positive regulation of transcription elongation by RNA polymerase II / helicase activity / double-strand break repair via homologous recombination / base-excision repair / chromatin DNA binding / double-strand break repair via nonhomologous end joining / G2/M transition of mitotic cell cycle / double-strand break repair / histone binding / sequence-specific DNA binding / DNA helicase / DNA-binding transcription factor activity, RNA polymerase II-specific / chromatin remodeling / chromatin binding / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / chromatin / positive regulation of DNA-templated transcription / structural molecule activity / positive regulation of transcription by RNA polymerase II / ATP hydrolysis activity / DNA binding / zinc ion binding / ATP binding / nucleus Similarity search - Function | |||||||||||||||||||||||||||||||||||||||||||||
| Biological species | ![]() | |||||||||||||||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.07 Å | |||||||||||||||||||||||||||||||||||||||||||||
Authors | Patel, A.B. / Moore, C.M. / Greber, B.J. / Nogales, E. | |||||||||||||||||||||||||||||||||||||||||||||
| Funding support | United States, 3items
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Citation | Journal: Elife / Year: 2019Title: Architecture of the chromatin remodeler RSC and insights into its nucleosome engagement. Authors: Avinash B Patel / Camille M Moore / Basil J Greber / Jie Luo / Stefan A Zukin / Jeff Ranish / Eva Nogales / ![]() Abstract: Eukaryotic DNA is packaged into nucleosome arrays, which are repositioned by chromatin remodeling complexes to control DNA accessibility. The RSC (emodeling the tructure of hromatin) complex, a ...Eukaryotic DNA is packaged into nucleosome arrays, which are repositioned by chromatin remodeling complexes to control DNA accessibility. The RSC (emodeling the tructure of hromatin) complex, a member of the SWI/SNF chromatin remodeler family, plays critical roles in genome maintenance, transcription, and DNA repair. Here, we report cryo-electron microscopy (cryo-EM) and crosslinking mass spectrometry (CLMS) studies of yeast RSC complex and show that RSC is composed of a rigid tripartite core and two flexible lobes. The core structure is scaffolded by an asymmetric Rsc8 dimer and built with the evolutionarily conserved subunits Sfh1, Rsc6, Rsc9 and Sth1. The flexible ATPase lobe, composed of helicase subunit Sth1, Arp7, Arp9 and Rtt102, is anchored to this core by the N-terminus of Sth1. Our cryo-EM analysis of RSC bound to a nucleosome core particle shows that in addition to the expected nucleosome-Sth1 interactions, RSC engages histones and nucleosomal DNA through one arm of the core structure, composed of the Rsc8 SWIRM domains, Sfh1 and Npl6. Our findings provide structural insights into the conserved assembly process for all members of the SWI/SNF family of remodelers, and illustrate how RSC selects, engages, and remodels nucleosomes. | |||||||||||||||||||||||||||||||||||||||||||||
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Structure visualization
| Movie |
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 6v8o.cif.gz | 681 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb6v8o.ent.gz | 483.5 KB | Display | PDB format |
| PDBx/mmJSON format | 6v8o.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 6v8o_validation.pdf.gz | 1.4 MB | Display | wwPDB validaton report |
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| Full document | 6v8o_full_validation.pdf.gz | 1.4 MB | Display | |
| Data in XML | 6v8o_validation.xml.gz | 88.8 KB | Display | |
| Data in CIF | 6v8o_validation.cif.gz | 139 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v8/6v8o ftp://data.pdbj.org/pub/pdb/validation_reports/v8/6v8o | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 21107MC ![]() 6v92C M: map data used to model this data C: citing same article ( |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-Protein , 2 types, 2 molecules CR
| #1: Protein | Mass: 9192.524 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q9URQ5 |
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| #12: Protein | Mass: 156982.406 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P32597, DNA helicase |
-Chromatin structure-remodeling complex protein ... , 6 types, 9 molecules DGIJKLMOS
| #2: Protein | Mass: 19825.398 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P38210 | ||||||
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| #5: Protein | Mass: 101819.938 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q06639 | ||||||
| #7: Protein | Mass: 63253.965 Da / Num. of mol.: 4 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P43609 #8: Protein | | Mass: 54222.691 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P25632 #10: Protein | | Mass: 57871.309 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q07979 #13: Protein | | Mass: 101448.211 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P38781 |
-Chromatin structure-remodeling complex subunit ... , 5 types, 5 molecules EFHNQ
| #3: Protein | Mass: 49716.520 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: P32832 |
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| #4: Protein | Mass: 102443.664 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q06488 |
| #6: Protein | Mass: 72372.375 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q02206 |
| #9: Protein | Mass: 65289.309 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q03124 |
| #11: Protein | Mass: 48833.180 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c / References: UniProt: Q06168 |
-Protein/peptide , 5 types, 6 molecules 234567
| #14: Protein/peptide | Mass: 2400.951 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c | ||||||
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| #15: Protein/peptide | Mass: 1635.006 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c #16: Protein/peptide | | Mass: 1209.482 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c #17: Protein/peptide | | Mass: 1294.587 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c #18: Protein/peptide | | Mass: 4188.154 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: ATCC 204508 / S288c |
-Non-polymers , 1 types, 1 molecules 
| #19: Chemical | ChemComp-ZN / |
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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
| Component | Name: Remodeling the Structure of Chromatin (RSC) / Type: COMPLEX / Entity ID: #1-#18 / Source: NATURAL |
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| Molecular weight | Value: 1.1 MDa / Experimental value: NO |
| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.9 |
| 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: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD |
| Image recording | Electron dose: 40 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
| Software | Name: PHENIX / Version: 1.17.1_3660: / Classification: refinement | ||||||||||||||||||||||||
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| EM software |
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.07 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 1920066 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi






United States, 3items
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