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- EMDB-6241: The Structure of a Biologically Active Estrogen Receptor-Coactiva... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-6241 | |||||||||
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Title | The Structure of a Biologically Active Estrogen Receptor-Coactivator Complex on DNA | |||||||||
![]() | ERa/SRC-3/p300 complex | |||||||||
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![]() | Estrogen receptor | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 25.0 Å | |||||||||
![]() | Yi P / Wang Z / Feng Q / Pintilie GD / Foulds CE / Lanz RB / Ludtke SJ / Schmid MF / Chiu W / O'Malley BW | |||||||||
![]() | ![]() Title: Structure of a biologically active estrogen receptor-coactivator complex on DNA. Authors: Ping Yi / Zhao Wang / Qin Feng / Grigore D Pintilie / Charles E Foulds / Rainer B Lanz / Steven J Ludtke / Michael F Schmid / Wah Chiu / Bert W O'Malley / ![]() Abstract: Estrogen receptor (ER/ESR1) is a transcription factor critical for development, reproduction, metabolism, and cancer. ER function hinges on its ability to recruit primary and secondary coactivators, ...Estrogen receptor (ER/ESR1) is a transcription factor critical for development, reproduction, metabolism, and cancer. ER function hinges on its ability to recruit primary and secondary coactivators, yet structural information on the full-length receptor-coactivator complex to complement preexisting and sometimes controversial biochemical information is lacking. Here, we use cryoelectron microscopy (cryo-EM) to determine the quaternary structure of an active complex of DNA-bound ERα, steroid receptor coactivator 3 (SRC-3/NCOA3), and a secondary coactivator (p300/EP300). Our structural model suggests the following assembly mechanism for the complex: each of the two ligand-bound ERα monomers independently recruits one SRC-3 protein via the transactivation domain of ERα; the two SRC-3s in turn bind to different regions of one p300 protein through multiple contacts. We also present structural evidence for the location of activation function 1 (AF-1) in a full-length nuclear receptor, which supports a role for AF-1 in SRC-3 recruitment. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 4.4 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 10.5 KB 10.5 KB | Display Display | ![]() |
Images | ![]() ![]() | 40.9 KB 3.9 KB | ||
Others | ![]() ![]() ![]() ![]() ![]() | 25.2 MB 1.8 MB 20 MB 5 MB 9.8 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 79.2 KB | Display | ![]() |
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Full document | ![]() | 78.3 KB | Display | |
Data in XML | ![]() | 493 B | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6259C ![]() 6260C ![]() 6261C ![]() 6262C ![]() 6263C ![]() 6264C C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Map
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Annotation | ERa/SRC-3/p300 complex | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 2.16 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Supplemental map: ER ab1.map
File | ER_ab1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Supplemental map: ER af1ab.map
File | ER_af1ab.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Supplemental map: p300-ab1.map
File | p300-ab1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Supplemental map: p300-ab2.map
File | p300-ab2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Supplemental map: p300.map
File | p300.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : ERa/SRC-3/p300 complex
Entire | Name: ERa/SRC-3/p300 complex |
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Components |
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-Supramolecule #1000: ERa/SRC-3/p300 complex
Supramolecule | Name: ERa/SRC-3/p300 complex / type: sample / ID: 1000 / Number unique components: 3 |
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Molecular weight | Experimental: 800 KDa / Theoretical: 770 KDa / Method: Sedimentation |
-Macromolecule #1: estrogen receptor alpha
Macromolecule | Name: estrogen receptor alpha / type: protein_or_peptide / ID: 1 / Name.synonym: ERalpha / Recombinant expression: Yes |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() ![]() |
-Macromolecule #2: steroid receptor coactivator-3
Macromolecule | Name: steroid receptor coactivator-3 / type: protein_or_peptide / ID: 2 / Name.synonym: SRC-3 / Recombinant expression: Yes |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() ![]() |
-Macromolecule #3: p300
Macromolecule | Name: p300 / type: protein_or_peptide / ID: 3 / Recombinant expression: Yes |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() ![]() |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Grid | Details: continuous carbon film supported by a 200-mesh R1.2/1.3 Quantifoil grid |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Instrument: FEI VITROBOT MARK IV / Method: Blot 1 second prior to plunging. |
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Electron microscopy
Microscope | JEOL 3200FSC |
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Alignment procedure | Legacy - Astigmatism: Objective lens astigmatism was corrected at 100,000 times magnification. |
Date | Oct 1, 2012 |
Image recording | Category: CCD / Film or detector model: GATAN ULTRASCAN 4000 (4k x 4k) / Digitization - Sampling interval: 15 µm / Number real images: 806 / Average electron dose: 25 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal magnification: 50000 |
Sample stage | Specimen holder model: GATAN LIQUID NITROGEN |
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Image processing
Details | Refinements were carried out with a final search angle of 2 degrees using the e2refine.py program. |
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CTF correction | Details: per image |
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 25.0 Å / Resolution method: OTHER / Software - Name: EMAN2 / Number images used: 18120 |
Final angle assignment | Details: EMAN2: final search angle 2 degrees |