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Yorodumi- PDB-8t1i: Atomic model of the mammalian Mediator complex with MED26 subunit -
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Open data
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Basic information
| Entry | Database: PDB / ID: 8t1i | |||||||||
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| Title | Atomic model of the mammalian Mediator complex with MED26 subunit | |||||||||
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Keywords | GENE REGULATION / mouse mediator / complex / MED26 subunit | |||||||||
| Function / homology | Function and homology informationpositive regulation of T cell extravasation / enucleate erythrocyte development / mammary gland branching involved in thelarche / positive regulation of type II interferon-mediated signaling pathway / positive regulation of mediator complex assembly / positive regulation of G0 to G1 transition / negative regulation of smooth muscle cell differentiation / Nuclear Receptor transcription pathway / regulation of vitamin D receptor signaling pathway / core mediator complex ...positive regulation of T cell extravasation / enucleate erythrocyte development / mammary gland branching involved in thelarche / positive regulation of type II interferon-mediated signaling pathway / positive regulation of mediator complex assembly / positive regulation of G0 to G1 transition / negative regulation of smooth muscle cell differentiation / Nuclear Receptor transcription pathway / regulation of vitamin D receptor signaling pathway / core mediator complex / retinal pigment epithelium development / embryonic hindlimb morphogenesis / androgen biosynthetic process / regulation of RNA biosynthetic process / Regulation of lipid metabolism by PPARalpha / blastocyst development / thyroid hormone receptor signaling pathway / thyroid hormone generation / Cytoprotection by HMOX1 / positive regulation of hepatocyte proliferation / embryonic heart tube development / Estrogen-dependent gene expression / lens development in camera-type eye / camera-type eye development / positive regulation of keratinocyte differentiation / ventricular trabecula myocardium morphogenesis / megakaryocyte development / mediator complex / nuclear retinoic acid receptor binding / cellular response to hepatocyte growth factor stimulus / positive regulation of intracellular estrogen receptor signaling pathway / embryonic hemopoiesis / cellular response to thyroid hormone stimulus / mammary gland epithelial cell proliferation / peroxisome proliferator activated receptor binding / nuclear vitamin D receptor binding / nuclear thyroid hormone receptor binding / negative regulation of neuron differentiation / epithelial cell proliferation involved in mammary gland duct elongation / stem cell population maintenance / cellular response to steroid hormone stimulus / cortical actin cytoskeleton / mammary gland branching involved in pregnancy / histone acetyltransferase activity / histone acetyltransferase binding / LBD domain binding / limb development / embryonic placenta development / skeletal muscle cell differentiation / animal organ regeneration / monocyte differentiation / nuclear receptor-mediated steroid hormone signaling pathway / keratinocyte differentiation / negative regulation of keratinocyte proliferation / positive regulation of transcription initiation by RNA polymerase II / general transcription initiation factor binding / negative regulation of fibroblast proliferation / fat cell differentiation / nuclear retinoid X receptor binding / ubiquitin ligase complex / erythrocyte development / lactation / RNA polymerase II preinitiation complex assembly / peroxisome proliferator activated receptor signaling pathway / positive regulation of erythrocyte differentiation / animal organ morphogenesis / liver development / cellular response to epidermal growth factor stimulus / nuclear estrogen receptor binding / nuclear receptor binding / brain development / transcription coregulator activity / positive regulation of transcription elongation by RNA polymerase II / promoter-specific chromatin binding / protein import into nucleus / cell morphogenesis / chromatin DNA binding / protein-DNA complex / mRNA transcription by RNA polymerase II / transcription coactivator binding / in utero embryonic development / heart development / transcription corepressor activity / ubiquitin protein ligase activity / transcription by RNA polymerase II / actin binding / angiogenesis / transcription regulator complex / DNA-binding transcription factor binding / RNA polymerase II-specific DNA-binding transcription factor binding / cytoskeleton / nuclear body / transcription coactivator activity / RNA polymerase II cis-regulatory region sequence-specific DNA binding / protein ubiquitination / positive regulation of gene expression / chromatin binding / positive regulation of cell population proliferation / regulation of transcription by RNA polymerase II / regulation of DNA-templated transcription Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.68 Å | |||||||||
Authors | Zhao, H. / Asturias, F. | |||||||||
| Funding support | United States, 2items
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Citation | Journal: Mol Cell / Year: 2024Title: An IDR-dependent mechanism for nuclear receptor control of Mediator interaction with RNA polymerase II. Authors: Haiyan Zhao / Jiaqin Li / Yufei Xiang / Sohail Malik / Supriya V Vartak / Giovana M B Veronezi / Natalie Young / McKayla Riney / Jens Kalchschmidt / Andrea Conte / Seol Kyoung Jung / ...Authors: Haiyan Zhao / Jiaqin Li / Yufei Xiang / Sohail Malik / Supriya V Vartak / Giovana M B Veronezi / Natalie Young / McKayla Riney / Jens Kalchschmidt / Andrea Conte / Seol Kyoung Jung / Srinivas Ramachandran / Robert G Roeder / Yi Shi / Rafael Casellas / Francisco J Asturias / ![]() Abstract: The essential Mediator (MED) coactivator complex plays a well-understood role in regulation of basal transcription in all eukaryotes, but the mechanism underlying its role in activator-dependent ...The essential Mediator (MED) coactivator complex plays a well-understood role in regulation of basal transcription in all eukaryotes, but the mechanism underlying its role in activator-dependent transcription remains unknown. We investigated modulation of metazoan MED interaction with RNA polymerase II (RNA Pol II) by antagonistic effects of the MED26 subunit and the CDK8 kinase module (CKM). Biochemical analysis of CKM-MED showed that the CKM blocks binding of the RNA Pol II carboxy-terminal domain (CTD), preventing RNA Pol II interaction. This restriction is eliminated by nuclear receptor (NR) binding to CKM-MED, which enables CTD binding in a MED26-dependent manner. Cryoelectron microscopy (cryo-EM) and crosslinking-mass spectrometry (XL-MS) revealed that the structural basis for modulation of CTD interaction with MED relates to a large intrinsically disordered region (IDR) in CKM subunit MED13 that blocks MED26 and CTD interaction with MED but is repositioned upon NR binding. Hence, NRs can control transcription initiation by priming CKM-MED for MED26-dependent RNA Pol II interaction. | |||||||||
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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 | 8t1i.cif.gz | 1.3 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb8t1i.ent.gz | 956.4 KB | Display | PDB format |
| PDBx/mmJSON format | 8t1i.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/t1/8t1i ftp://data.pdbj.org/pub/pdb/validation_reports/t1/8t1i | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 40968MC ![]() 8t1lC ![]() 8t9dC 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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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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Components
+Mediator of RNA polymerase II transcription subunit ... , 26 types, 26 molecules ABCDEFGHIJKLMNOPQRSTUVWXYZ
-Protein/peptide , 1 types, 1 molecules a
| #27: Protein/peptide | Mass: 1720.111 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Details
| Has protein modification | 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: Mouse mediator complex / Type: COMPLEX / Entity ID: all / Source: NATURAL |
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| Molecular weight | Value: 1.0 MDa / Experimental value: NO |
| Source (natural) | Organism: ![]() |
| Buffer solution | pH: 7.9 |
| Specimen | Conc.: 0.1 mg/ml / Embedding applied: YES / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| EM embedding | Material: ice |
| Vitrification | Instrument: HOMEMADE PLUNGER / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277 K |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TALOS ARCTICA |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 3500 nm / Nominal defocus min: 700 nm / Cs: 2.7 mm / C2 aperture diameter: 50 µm |
| Image recording | Electron dose: 22.5 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Version: dev_3758: / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: NONE | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 4.68 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 199078 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi





United States, 2items
Citation






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FIELD EMISSION GUN