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Open data
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Basic information
| Entry | Database: PDB / ID: 6lth | ||||||
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| Title | Structure of human BAF Base module | ||||||
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Keywords | GENE REGULATION / Chromatin remodeler / Complex | ||||||
| Function / homology | Function and homology informationnegative regulation of myeloid progenitor cell differentiation / single stranded viral RNA replication via double stranded DNA intermediate / Positive Regulation of CDH1 Gene Transcription / brahma complex / positive regulation of glucose mediated signaling pathway / nBAF complex / npBAF complex / negative regulation of androgen receptor signaling pathway / positive regulation of transcription of nucleolar large rRNA by RNA polymerase I / neural retina development ...negative regulation of myeloid progenitor cell differentiation / single stranded viral RNA replication via double stranded DNA intermediate / Positive Regulation of CDH1 Gene Transcription / brahma complex / positive regulation of glucose mediated signaling pathway / nBAF complex / npBAF complex / negative regulation of androgen receptor signaling pathway / positive regulation of transcription of nucleolar large rRNA by RNA polymerase I / neural retina development / N-acetyltransferase activity / Formation of the embryonic stem cell BAF (esBAF) complex / EGR2 and SOX10-mediated initiation of Schwann cell myelination / Formation of the canonical BAF (cBAF) complex / Formation of the polybromo-BAF (pBAF) complex / Formation of neuronal progenitor and neuronal BAF (npBAF and nBAF) / Formation of the non-canonical BAF (ncBAF) complex / nucleosome array spacer activity / histone H3K14ac reader activity / regulation of G0 to G1 transition / Tat protein binding / RNA polymerase I preinitiation complex assembly / XY body / cellular response to fatty acid / host-mediated activation of viral transcription / SWI/SNF complex / ATP-dependent chromatin remodeler activity / nucleosome disassembly / regulation of mitotic metaphase/anaphase transition / nuclear androgen receptor binding / positive regulation of T cell differentiation / regulation of nucleotide-excision repair / nuclear chromosome / positive regulation of stem cell population maintenance / positive regulation of double-strand break repair / Regulation of MITF-M-dependent genes involved in pigmentation / negative regulation of cell differentiation / RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known / histone H4K16ac reader activity / positive regulation of myoblast differentiation / ATP-dependent activity, acting on DNA / positive regulation of Wnt signaling pathway / positive regulation of signal transduction by p53 class mediator / regulation of G1/S transition of mitotic cell cycle / Chromatin modifying enzymes / DNA polymerase binding / apoptotic signaling pathway / Interleukin-7 signaling / transcription initiation-coupled chromatin remodeling / nuclear receptor binding / transcription coregulator binding / helicase activity / positive regulation of cell differentiation / Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) / DNA integration / negative regulation of cell growth / positive regulation of miRNA transcription / fibrillar center / Negative Regulation of CDH1 Gene Transcription / Formation of the beta-catenin:TCF transactivating complex / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / transcription coregulator activity / kinetochore / nuclear matrix / RMTs methylate histone arginines / p53 binding / transcription corepressor activity / positive regulation of cold-induced thermogenesis / nervous system development / heterochromatin formation / histone binding / molecular adaptor activity / transcription coactivator activity / chromatin remodeling / signaling receptor binding / negative regulation of DNA-templated transcription / apoptotic process / positive regulation of cell population proliferation / chromatin binding / regulation of transcription by RNA polymerase II / nucleolus / regulation of DNA-templated transcription / positive regulation of DNA-templated transcription / chromatin / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / ATP hydrolysis activity / protein-containing complex / DNA binding / : / DNA-templated transcription / RNA binding / nucleoplasm / zinc ion binding / ATP binding / membrane / identical protein binding / nucleus / cytosol Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3 Å | ||||||
Authors | He, S. / Wu, Z. / Tian, Y. / Yu, Z. / Yu, J. / Wang, X. / Li, J. / Liu, B. / Xu, Y. | ||||||
Citation | Journal: Science / Year: 2020Title: Structure of nucleosome-bound human BAF complex. Authors: Shuang He / Zihan Wu / Yuan Tian / Zishuo Yu / Jiali Yu / Xinxin Wang / Jie Li / Bijun Liu / Yanhui Xu / ![]() Abstract: Mammalian SWI/SNF family chromatin remodelers, BRG1/BRM-associated factor (BAF) and polybromo-associated BAF (PBAF), regulate chromatin structure and transcription, and their mutations are linked to ...Mammalian SWI/SNF family chromatin remodelers, BRG1/BRM-associated factor (BAF) and polybromo-associated BAF (PBAF), regulate chromatin structure and transcription, and their mutations are linked to cancers. The 3.7-angstrom-resolution cryo-electron microscopy structure of human BAF bound to the nucleosome reveals that the nucleosome is sandwiched by the base and the adenosine triphosphatase (ATPase) modules, which are bridged by the actin-related protein (ARP) module. The ATPase motor is positioned proximal to nucleosomal DNA and, upon ATP hydrolysis, engages with and pumps DNA along the nucleosome. The C-terminal α helix of SMARCB1, enriched in positively charged residues frequently mutated in cancers, mediates interactions with an acidic patch of the nucleosome. AT-rich interactive domain-containing protein 1A (ARID1A) and the SWI/SNF complex subunit SMARCC serve as a structural core and scaffold in the base module organization, respectively. Our study provides structural insights into subunit organization and nucleosome recognition of human BAF complex. | ||||||
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Structure visualization
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 6lth.cif.gz | 459.5 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb6lth.ent.gz | 299.6 KB | Display | PDB format |
| PDBx/mmJSON format | 6lth.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lt/6lth ftp://data.pdbj.org/pub/pdb/validation_reports/lt/6lth | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 0968MC ![]() 0969C ![]() 0970C ![]() 0971C ![]() 0972C ![]() 0973C ![]() 0974C ![]() 6ltjC C: citing same article ( M: map data used to model this data |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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Components
-Protein , 4 types, 5 molecules ILNOR
| #1: Protein | Mass: 184923.828 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SMARCA4 / Cell line (production host): HEK293T / Production host: Homo sapiens (human)References: UniProt: P51532, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement | ||
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| #2: Protein | Mass: 242250.312 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ARID1A / Cell line (production host): HEK293T / Production host: Homo sapiens (human) / References: UniProt: O14497 | ||
| #4: Protein | Mass: 133048.109 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SMARCC2 / Cell line (production host): HEK293T / Production host: Homo sapiens (human) / References: UniProt: Q8TAQ2#7: Protein | | Mass: 44222.547 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DPF2 / Cell line (production host): HEK293T / Production host: Homo sapiens (human) / References: UniProt: Q92785 |
-SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily ... , 3 types, 3 molecules MPQ
| #3: Protein | Mass: 44199.188 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SMARCB1 / Cell line (production host): HEK293T / Production host: Homo sapiens (human) / References: UniProt: Q12824 |
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| #5: Protein | Mass: 58311.391 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SMARCD1 / Cell line (production host): HEK293T / Production host: Homo sapiens (human) / References: UniProt: Q96GM5 |
| #6: Protein | Mass: 46710.371 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SMARCE1 / Cell line (production host): HEK293T / Production host: Homo sapiens (human) / References: UniProt: Q969G3 |
-Non-polymers , 1 types, 1 molecules 
| #8: Chemical | ChemComp-ZN / |
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-Details
| Has ligand of interest | Y |
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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 |
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Sample preparation
| Component | Name: Structure of human BAF Base module / Type: COMPLEX / Entity ID: #1-#7 / Source: RECOMBINANT |
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| Molecular weight | Units: KILODALTONS/NANOMETER / Experimental value: NO |
| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: Homo sapiens (human) / Cell: HEK293T |
| Buffer solution | pH: 8 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3 |
| Vitrification | Cryogen name: ETHANE / Humidity: 100 % |
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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: OTHER |
| Specimen holder | Cryogen: NITROGEN |
| Image recording | Electron dose: 50 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: GATAN K2 SUMMIT (4k x 4k) |
| EM imaging optics | Energyfilter slit width: 20 eV |
| Image scans | Movie frames/image: 32 / Used frames/image: 1-32 |
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Processing
| Software | Name: PHENIX / Version: 1.16_3549: / Classification: refinement | ||||||||||||||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||||||||||||||
| Symmetry | Point symmetry: C1 (asymmetric) | ||||||||||||||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 197606 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||||||
| Atomic model building | Protocol: AB INITIO MODEL / Space: REAL | ||||||||||||||||||||||||||||||||||||
| Refine LS restraints |
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