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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 | ||||||
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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 / negative regulation of smooth muscle cell differentiation / core mediator complex / androgen biosynthetic process / regulation of RNA biosynthetic process / retinal pigment epithelium development / thyroid hormone receptor signaling pathway / positive regulation of keratinocyte differentiation / ventricular trabecula myocardium morphogenesis ...positive regulation of mediator complex assembly / CKM complex / negative regulation of smooth muscle cell differentiation / core mediator complex / androgen biosynthetic process / regulation of RNA biosynthetic process / retinal pigment epithelium development / thyroid hormone receptor signaling pathway / positive regulation of keratinocyte differentiation / ventricular trabecula myocardium morphogenesis / mediator complex / Generic Transcription Pathway / nuclear retinoic acid receptor binding / positive regulation of chromatin binding / lens development in camera-type eye / cellular response to thyroid hormone stimulus / megakaryocyte development / nuclear vitamin D receptor binding / peroxisome proliferator activated receptor binding / nuclear thyroid hormone receptor binding / triglyceride homeostasis / cellular response to steroid hormone stimulus / negative regulation of neuron differentiation / cortical actin cytoskeleton / limb development / histone acetyltransferase binding / LBD domain binding / RSV-host interactions / blastocyst development / skeletal muscle cell differentiation / somatic stem cell population maintenance / nuclear receptor-mediated steroid hormone signaling pathway / negative regulation of keratinocyte proliferation / keratinocyte differentiation / general transcription initiation factor binding / positive regulation of transcription initiation by RNA polymerase II / fat cell differentiation / nuclear retinoid X receptor binding / ubiquitin ligase complex / negative regulation of fibroblast proliferation / RNA polymerase II preinitiation complex assembly / erythrocyte development / Regulation of lipid metabolism by PPARalpha / BMAL1:CLOCK,NPAS2 activates circadian expression / RORA,B,C and NR1D1 (REV-ERBA) regulate gene expression / Activation of gene expression by SREBF (SREBP) / Expression of BMAL (ARNTL), CLOCK, and NPAS2 / positive regulation of erythrocyte differentiation / cholesterol homeostasis / cellular response to epidermal growth factor stimulus / nuclear estrogen receptor binding / nuclear receptor binding / transcription coregulator activity / Heme signaling / positive regulation of transcription elongation by RNA polymerase II / transcription initiation at RNA polymerase II promoter / PPARA activates gene expression / promoter-specific chromatin binding / Transcriptional activation of mitochondrial biogenesis / Cytoprotection by HMOX1 / Nuclear Receptor transcription pathway / protein-DNA complex / Transcriptional regulation of white adipocyte differentiation / chromatin DNA binding / mRNA transcription by RNA polymerase II / cell morphogenesis / transcription coactivator binding / 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 / actin binding / transcription by RNA polymerase II / angiogenesis / transcription regulator complex / Estrogen-dependent gene expression / DNA-binding transcription factor binding / transcription coactivator activity / nuclear body / RNA polymerase II cis-regulatory region sequence-specific DNA binding / protein ubiquitination / chromatin binding / positive regulation of gene expression / regulation of transcription by RNA polymerase II / regulation of DNA-templated transcription / negative regulation of apoptotic process / nucleolus / positive regulation of DNA-templated transcription / chromatin / protein-containing complex binding / negative regulation of transcription by RNA polymerase II / DNA-templated transcription / positive regulation of transcription by RNA polymerase II / DNA binding / nucleoplasm / membrane / nucleus / cytosol / 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