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Open data
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Basic information
| Entry | Database: PDB / ID: 9c4b | |||||||||||||||
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| Title | Second BAF53a of the human TIP60 complex | |||||||||||||||
Components | Actin-like protein 6A | |||||||||||||||
Keywords | GENE REGULATION / Chromatin Modification | |||||||||||||||
| Function / homology | Function and homology informationregulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / neural retina development / npBAF complex / brahma complex / GBAF complex / regulation of G0 to G1 transition / Ino80 complex / blastocyst formation / RSC-type complex ...regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / neural retina development / npBAF complex / brahma complex / GBAF complex / regulation of G0 to G1 transition / Ino80 complex / blastocyst formation / RSC-type complex / regulation of double-strand break repair / regulation of nucleotide-excision repair / SWI/SNF complex / regulation of mitotic metaphase/anaphase transition / positive regulation of T cell differentiation / positive regulation of double-strand break repair / spinal cord development / regulation of chromosome organization / NuA4 histone acetyltransferase complex / RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known / positive regulation of stem cell population maintenance / Regulation of MITF-M-dependent genes involved in pigmentation / regulation of DNA replication / regulation of G1/S transition of mitotic cell cycle / regulation of embryonic development / negative regulation of cell differentiation / positive regulation of myoblast differentiation / regulation of DNA repair / positive regulation of double-strand break repair via homologous recombination / telomere maintenance / positive regulation of DNA repair / positive regulation of cell differentiation / Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) / DNA Damage Recognition in GG-NER / kinetochore / RMTs methylate histone arginines / nuclear matrix / UCH proteinases / nervous system development / nucleosome / HATs acetylate histones / regulation of apoptotic process / DNA recombination / transcription coactivator activity / regulation of cell cycle / chromatin remodeling / DNA repair / positive regulation of cell population proliferation / chromatin binding / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / chromatin / positive regulation of DNA-templated transcription / signal transduction / protein-containing complex / nucleoplasm / nucleus / plasma membrane Similarity search - Function | |||||||||||||||
| Biological species | Homo sapiens (human) | |||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å | |||||||||||||||
Authors | Yang, Z. / Mameri, A. / Florez Ariza, A.J. / Cote, J. / Nogales, E. | |||||||||||||||
| Funding support | United States, Canada, 4items
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Citation | Journal: Science / Year: 2024Title: Structural insights into the human NuA4/TIP60 acetyltransferase and chromatin remodeling complex. Authors: Zhenlin Yang / Amel Mameri / Claudia Cattoglio / Catherine Lachance / Alfredo Jose Florez Ariza / Jie Luo / Jonathan Humbert / Deepthi Sudarshan / Arul Banerjea / Maxime Galloy / Amélie ...Authors: Zhenlin Yang / Amel Mameri / Claudia Cattoglio / Catherine Lachance / Alfredo Jose Florez Ariza / Jie Luo / Jonathan Humbert / Deepthi Sudarshan / Arul Banerjea / Maxime Galloy / Amélie Fradet-Turcotte / Jean-Philippe Lambert / Jeff A Ranish / Jacques Côté / Eva Nogales / ![]() Abstract: The human nucleosome acetyltransferase of histone H4 (NuA4)/Tat-interactive protein, 60 kilodalton (TIP60) coactivator complex, a fusion of the yeast switch/sucrose nonfermentable related 1 (SWR1) ...The human nucleosome acetyltransferase of histone H4 (NuA4)/Tat-interactive protein, 60 kilodalton (TIP60) coactivator complex, a fusion of the yeast switch/sucrose nonfermentable related 1 (SWR1) and NuA4 complexes, both incorporates the histone variant H2A.Z into nucleosomes and acetylates histones H4, H2A, and H2A.Z to regulate gene expression and maintain genome stability. Our cryo-electron microscopy studies show that, within the NuA4/TIP60 complex, the E1A binding protein P400 (EP400) subunit serves as a scaffold holding the different functional modules in specific positions, creating a distinct arrangement of the actin-related protein (ARP) module. EP400 interacts with the transformation/transcription domain-associated protein (TRRAP) subunit by using a footprint that overlaps with that of the Spt-Ada-Gcn5 acetyltransferase (SAGA) complex, preventing the formation of a hybrid complex. Loss of the TRRAP subunit leads to mislocalization of NuA4/TIP60, resulting in the redistribution of H2A.Z and its acetylation across the genome, emphasizing the dual functionality of NuA4/TIP60 as a single macromolecular assembly. | |||||||||||||||
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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 | 9c4b.cif.gz | 153.7 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9c4b.ent.gz | 123.4 KB | Display | PDB format |
| PDBx/mmJSON format | 9c4b.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9c4b_validation.pdf.gz | 1.2 MB | Display | wwPDB validaton report |
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| Full document | 9c4b_full_validation.pdf.gz | 1.2 MB | Display | |
| Data in XML | 9c4b_validation.xml.gz | 26.5 KB | Display | |
| Data in CIF | 9c4b_validation.cif.gz | 35.1 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c4/9c4b ftp://data.pdbj.org/pub/pdb/validation_reports/c4/9c4b | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 45180MC ![]() 9c47C ![]() 9c57C ![]() 9c62C ![]() 9c6nC 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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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 47509.812 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ACTL6A, BAF53, BAF53A, INO80K / Production host: Homo sapiens (human) / References: UniProt: O96019 |
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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: Second BAF53a of the human TIP60 complex / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.5 |
| 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: SPOT SCAN |
| Electron lens | Mode: 4D-STEM / Nominal defocus max: 2500 nm / Nominal defocus min: 1000 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (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: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 96931 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi




Homo sapiens (human)
United States,
Canada, 4items
Citation








PDBj






FIELD EMISSION GUN