+
Open data
-
Basic information
Entry | Database: PDB / ID: 7yfn | ||||||
---|---|---|---|---|---|---|---|
Title | Core module of the NuA4 complex in S. cerevisiae | ||||||
![]() |
| ||||||
![]() | TRANSFERASE / histone / acetyltransferase / H4 / NuA4 | ||||||
Function / homology | ![]() : / RHOB GTPase cycle / : / RHOA GTPase cycle / cellular bud neck contractile ring / piccolo histone acetyltransferase complex / ascospore wall assembly / vacuole inheritance / actin cortical patch / mitotic actomyosin contractile ring contraction ...: / RHOB GTPase cycle / : / RHOA GTPase cycle / cellular bud neck contractile ring / piccolo histone acetyltransferase complex / ascospore wall assembly / vacuole inheritance / actin cortical patch / mitotic actomyosin contractile ring contraction / Swr1 complex / SLIK (SAGA-like) complex / Ino80 complex / SAGA complex / intracellular non-membrane-bounded organelle / establishment of cell polarity / NuA4 histone acetyltransferase complex / actin filament bundle / positive regulation of macroautophagy / protein secretion / Ub-specific processing proteases / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / structural constituent of cytoskeleton / endocytosis / nucleosome / chromatin organization / hydrolase activity / chromatin remodeling / cell cycle / DNA repair / DNA-templated transcription / regulation of DNA-templated transcription / chromatin / regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / ATP binding / identical protein binding / nucleus Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.8 Å | ||||||
![]() | Ji, L.T. / Zhao, L.X. / Xu, K. / Gao, H.H. / Zhou, Y. / Kornberg, R.D. / Zhang, H.Q. | ||||||
Funding support | ![]()
| ||||||
![]() | ![]() Title: Structure of the NuA4 histone acetyltransferase complex. Authors: Liting Ji / Lixia Zhao / Ke Xu / Huihan Gao / Yang Zhou / Roger D Kornberg / Heqiao Zhang / ![]() ![]() Abstract: Nucleosome acetyltransferase of H4 (NuA4), one of two major histone acetyltransferase complexes in specifically acetylates histone H2A and H4, resulting in increased transcriptional activity. Here ...Nucleosome acetyltransferase of H4 (NuA4), one of two major histone acetyltransferase complexes in specifically acetylates histone H2A and H4, resulting in increased transcriptional activity. Here we present a 3.8-4.0 Å resolution structure of the NuA4 complex from cryoelectron microscopy and associated biochemical studies. The determined structure comprises six subunits and appropriately 5,000 amino acids, with a backbone formed by subunits Eaf1 and Eaf2 spanning from an Actin-Arp4 module to a platform subunit Tra1. Seven subunits are missing from the cryo-EM map. The locations of missing components, Yaf9, and three subunits of the Piccolo module Esa1, Yng2, and Eaf6 were determined. Biochemical studies showed that the Piccolo module and the complete NuA4 exhibit comparable histone acetyltransferase activities, but the Piccolo module binds to nucleosomes, whereas the complete NuA4 does not. The interaction lifetime of NuA4 and nucleosome is evidently short, possibly because of subunits of the NuA4 complex that diminish the affinity of the Piccolo module for the nucleosome, enabling rapid movement from nucleosome to nucleosome. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 657.9 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 492.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.5 MB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 1.6 MB | Display | |
Data in XML | ![]() | 112.2 KB | Display | |
Data in CIF | ![]() | 164 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 33794MC ![]() 7yfpC M: map data used to model this data C: citing same article ( |
---|---|
Similar structure data | Similarity search - Function & homology ![]() |
-
Links
-
Assembly
Deposited unit | ![]()
|
---|---|
1 |
|
-
Components
-Protein , 6 types, 6 molecules ABDETF
#1: Protein | Mass: 41402.184 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 204508 / S288c / Gene: ACT1, ABY1, END7, YFL039C / Production host: ![]() ![]() |
---|---|
#2: Protein | Mass: 54894.684 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC 204508 / S288c / Gene: ARP4 / Production host: ![]() ![]() |
#3: Protein | Mass: 112667.008 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: EAF1 / Production host: ![]() ![]() |
#4: Protein | Mass: 55297.684 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: SWC4 / Production host: ![]() ![]() |
#5: Protein | Mass: 433677.281 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() |
#6: Protein | Mass: 96889.867 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: EPL1, YFL024C / Production host: ![]() ![]() |
-Non-polymers , 1 types, 1 molecules ![](data/chem/img/ATP.gif)
#7: Chemical | ChemComp-ATP / |
---|
-Details
Has ligand of interest | Y |
---|
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
---|---|
EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-
Sample preparation
Component | Name: Cryo-EM structure of NuA4 complex / Type: COMPLEX / Entity ID: #1-#6 / Source: NATURAL |
---|---|
Source (natural) | Organism: ![]() ![]() |
Buffer solution | pH: 8 |
Specimen | Conc.: 1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 301 K |
-
Electron microscopy imaging
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
---|---|
Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1300 nm |
Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-
Processing
Software | Name: PHENIX / Version: 1.17.1_3660: / Classification: refinement | ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 197044 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
|