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Open data
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Basic information
| Entry | Database: PDB / ID: 8t9d | ||||||
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| Title | CryoEM structure of TR-TRAP | ||||||
Components |
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Keywords | STRUCTURAL PROTEIN / TR-TRAP / mediator / CKM module | ||||||
| Function / homology | Function and homology informationpositive regulation of mediator complex assembly / CKM complex / retinal pigment epithelium development / androgen biosynthetic process / regulation of RNA biosynthetic process / thyroid hormone receptor signaling pathway / core mediator complex / lens development in camera-type eye / ventricular trabecula myocardium morphogenesis / megakaryocyte development ...positive regulation of mediator complex assembly / CKM complex / retinal pigment epithelium development / androgen biosynthetic process / regulation of RNA biosynthetic process / thyroid hormone receptor signaling pathway / core mediator complex / lens development in camera-type eye / ventricular trabecula myocardium morphogenesis / megakaryocyte development / negative regulation of keratinocyte proliferation / mediator complex / Generic Transcription Pathway / nuclear retinoic acid receptor binding / positive regulation of keratinocyte differentiation / positive regulation of chromatin binding / cellular response to thyroid hormone stimulus / nuclear vitamin D receptor binding / peroxisome proliferator activated receptor binding / nuclear thyroid hormone receptor binding / negative regulation of neuron differentiation / triglyceride homeostasis / cellular response to steroid hormone stimulus / cortical actin cytoskeleton / histone acetyltransferase binding / LBD domain binding / RSV-host interactions / erythrocyte development / keratinocyte differentiation / nuclear receptor-mediated steroid hormone signaling pathway / positive regulation of transcription initiation by RNA polymerase II / negative regulation of fibroblast proliferation / general transcription initiation factor binding / fat cell differentiation / nuclear retinoid X receptor binding / cell morphogenesis / RNA polymerase II preinitiation complex assembly / Regulation of lipid metabolism by PPARalpha / ubiquitin ligase complex / cholesterol homeostasis / positive regulation of erythrocyte differentiation / BMAL1:CLOCK,NPAS2 activates circadian expression / RORA,B,C and NR1D1 (REV-ERBA) regulate gene expression / Expression of BMAL (ARNTL), CLOCK, and NPAS2 / Activation of gene expression by SREBF (SREBP) / cellular response to epidermal growth factor stimulus / nuclear receptor binding / nuclear estrogen receptor binding / Heme signaling / positive regulation of transcription elongation by RNA polymerase II / PPARA activates gene expression / Cytoprotection by HMOX1 / Transcriptional activation of mitochondrial biogenesis / promoter-specific chromatin binding / transcription initiation at RNA polymerase II promoter / chromatin DNA binding / Transcriptional regulation of white adipocyte differentiation / Nuclear Receptor transcription pathway / protein-DNA complex / mRNA transcription by RNA polymerase II / transcription by RNA polymerase II / transcription coregulator activity / transcription coactivator binding / angiogenesis / transcription corepressor activity / DNA-directed RNA polymerase activity / ubiquitin protein ligase activity / MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesis and hepatic steatosis / transcription regulator complex / DNA-binding transcription factor binding / Estrogen-dependent gene expression / nuclear body / transcription coactivator activity / protein ubiquitination / RNA polymerase II cis-regulatory region sequence-specific DNA binding / chromatin binding / positive regulation of gene expression / regulation of transcription by RNA polymerase II / negative regulation of apoptotic process / nucleolus / regulation of DNA-templated transcription / positive regulation of DNA-templated transcription / chromatin / protein-containing complex binding / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / DNA-templated transcription / DNA binding / nucleoplasm / membrane / nucleus / cytoplasm Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.66 Å | ||||||
Authors | Zhao, H. / Asturias, F. | ||||||
| Funding support | United States, 1items
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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 | 8t9d.cif.gz | 1.3 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb8t9d.ent.gz | 955.4 KB | Display | PDB format |
| PDBx/mmJSON format | 8t9d.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/t9/8t9d ftp://data.pdbj.org/pub/pdb/validation_reports/t9/8t9d | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 41107MC ![]() 8t1iC ![]() 8t1lC 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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Components
+Mediator of RNA polymerase II transcription subunit ... , 25 types, 25 molecules ABCDEFGHIJKLMOPQRSTVWXYZ9
-Protein/peptide , 1 types, 1 molecules a
| #25: Protein/peptide | Mass: 1720.111 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) |
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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: mediator complex with transcription factor TR / Type: COMPLEX / Entity ID: all / Source: NATURAL |
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| Source (natural) | Organism: Homo sapiens (human) |
| Buffer solution | pH: 7.9 |
| 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: Talos Arctica / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TECNAI ARCTICA |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 35000 nm / Nominal defocus min: 800 nm |
| Image recording | Electron dose: 100 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
| CTF correction | Type: NONE |
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| 3D reconstruction | Resolution: 4.66 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 31505 / Symmetry type: POINT |
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About Yorodumi




Homo sapiens (human)
United States, 1items
Citation






PDBj








FIELD EMISSION GUN