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Yorodumi- PDB-7c4j: Cryo-EM structure of the yeast Swi/Snf complex in a nucleosome fr... -
+Open data
-Basic information
Entry | Database: PDB / ID: 7c4j | |||||||||
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Title | Cryo-EM structure of the yeast Swi/Snf complex in a nucleosome free state | |||||||||
Components |
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Keywords | DNA BINDING PROTEIN / SWI/SNF remodeling / Swi-Snf complex / nucleosome | |||||||||
Function / homology | Function and homology information carbon catabolite activation of transcription from RNA polymerase II promoter / positive regulation of cell adhesion involved in single-species biofilm formation / positive regulation of mating type switching / RHO GTPases activate IQGAPs / RHO GTPases Activate WASPs and WAVEs / Regulation of actin dynamics for phagocytic cup formation / positive regulation of invasive growth in response to glucose limitation / HDACs deacetylate histones / aggrephagy / Platelet degranulation ...carbon catabolite activation of transcription from RNA polymerase II promoter / positive regulation of cell adhesion involved in single-species biofilm formation / positive regulation of mating type switching / RHO GTPases activate IQGAPs / RHO GTPases Activate WASPs and WAVEs / Regulation of actin dynamics for phagocytic cup formation / positive regulation of invasive growth in response to glucose limitation / HDACs deacetylate histones / aggrephagy / Platelet degranulation / DNA strand invasion / rDNA binding / : / SUMOylation of chromatin organization proteins / nucleosome disassembly / RSC-type complex / SWI/SNF complex / ATP-dependent chromatin remodeler activity / nucleosomal DNA binding / NuA4 histone acetyltransferase complex / nuclear chromosome / positive regulation of transcription by RNA polymerase I / ATP-dependent activity, acting on DNA / maturation of LSU-rRNA / helicase activity / chromosome segregation / transcription elongation by RNA polymerase II / nucleotide-excision repair / double-strand break repair via homologous recombination / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / lysine-acetylated histone binding / DNA-templated DNA replication / chromatin DNA binding / double-strand break repair / chromatin organization / histone binding / RNA polymerase II-specific DNA-binding transcription factor binding / transcription cis-regulatory region binding / hydrolase activity / chromatin remodeling / chromatin binding / chromatin / structural molecule activity / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / positive regulation of DNA-templated transcription / positive regulation of transcription by RNA polymerase II / DNA binding / ATP binding / metal ion binding / nucleus / cytosol Similarity search - Function | |||||||||
Biological species | Saccharomyces cerevisiae S288C (yeast) | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.89 Å | |||||||||
Authors | Wang, C.C. / Guo, Z.Y. / Zhan, X.C. / Zhang, X.F. | |||||||||
Funding support | China, 2items
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Citation | Journal: Nat Commun / Year: 2020 Title: Structure of the yeast Swi/Snf complex in a nucleosome free state. Authors: Chengcheng Wang / Zhouyan Guo / Xiechao Zhan / Fenghua Yang / Mingxuan Wu / Xiaofeng Zhang / Abstract: SWI/SNF remodelers play a key role in regulating chromatin architecture and gene expression. Here, we report the cryo-EM structure of the Saccharomyces cerevisiae Swi/Snf complex in a nucleosome-free ...SWI/SNF remodelers play a key role in regulating chromatin architecture and gene expression. Here, we report the cryo-EM structure of the Saccharomyces cerevisiae Swi/Snf complex in a nucleosome-free state. The structure consists of a stable triangular base module and a flexible Arp module. The conserved subunits Swi1 and Swi3 form the backbone of the complex and closely interact with other components. Snf6, which is specific for yeast Swi/Snf complex, stabilizes the binding of the ATPase-containing subunit Snf2 to the base module. Comparison of the yeast Swi/Snf and RSC complexes reveals conserved structural features that govern the assembly and function of these two subfamilies of chromatin remodelers. Our findings complement those from recent structures of the yeast and human chromatin remodelers and provide further insights into the assembly and function of the SWI/SNF remodelers. | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | Molecule: MolmilJmol/JSmol |
-Downloads & links
-Download
PDBx/mmCIF format | 7c4j.cif.gz | 766.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7c4j.ent.gz | 571 KB | Display | PDB format |
PDBx/mmJSON format | 7c4j.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c4/7c4j ftp://data.pdbj.org/pub/pdb/validation_reports/c4/7c4j | HTTPS FTP |
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-Related structure data
Related structure data | 30285MC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
-Transcription regulatory protein ... , 3 types, 3 molecules ACH
#1: Protein | Mass: 63947.633 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae S288C (yeast) / Strain: S288c / References: UniProt: P53628 |
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#3: Protein | Mass: 37652.582 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae S288C (yeast) / Strain: S288c / References: UniProt: P18888 |
#6: Protein | Mass: 194315.094 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae S288C (yeast) / Strain: S288c References: UniProt: P22082, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement |
-Protein , 6 types, 7 molecules BDEGJKL
#2: Protein | Mass: 93034.164 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae S288C (yeast) / Strain: S288c / References: UniProt: P32591 #4: Protein | | Mass: 70366.617 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae S288C (yeast) / Strain: S288c / References: UniProt: P43554 #8: Protein | | Mass: 7600.243 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae S288C (yeast) / Strain: S288c #9: Protein | | Mass: 17817.615 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae S288C (yeast) / Strain: S288c / References: UniProt: P53330 #10: Protein | | Mass: 53863.016 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae S288C (yeast) / Strain: S288c / References: UniProt: Q12406 #11: Protein | | Mass: 53131.930 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae S288C (yeast) / Strain: S288c / References: UniProt: Q05123 |
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-SWI/SNF chromatin-remodeling complex subunit ... , 2 types, 2 molecules FI
#5: Protein | Mass: 102642.172 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae S288C (yeast) / Strain: S288c / References: UniProt: P18480 |
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#7: Protein | Mass: 148065.188 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Saccharomyces cerevisiae S288C (yeast) / Strain: S288c / References: UniProt: P09547 |
-Details
Sequence details | Authors state that the residues except Ala were basically generated from our EM map and seem like ...Authors state that the residues except Ala were basically generated from our EM map and seem like those side-chains for the chain G (unknown molecule). |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: the yeast Swi/Snf complex / Type: COMPLEX / Entity ID: all / Source: NATURAL |
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Molecular weight | Value: 1.14 MDa / Experimental value: NO |
Source (natural) | Organism: Saccharomyces cerevisiae S288C (yeast) / Strain: S288C |
Buffer solution | pH: 7.4 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-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 FIELDBright-field microscopy / Cs: 2.7 mm |
Specimen holder | Cryogen: NITROGEN |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-Processing
Software | Name: PHENIX / Version: 1.17.1_3660: / Classification: refinement | ||||||||||||||||||||||||
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CTF correction | Type: NONE | ||||||||||||||||||||||||
3D reconstruction | Resolution: 2.89 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 386469 / Symmetry type: POINT | ||||||||||||||||||||||||
Refinement | Highest resolution: 2.89 Å | ||||||||||||||||||||||||
Refine LS restraints |
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