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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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![]() | STRUCTURAL PROTEIN / TR-TRAP / mediator / CKM module | ||||||
Function / homology | ![]() positive regulation of mediator complex assembly / positive regulation of T cell extravasation / positive regulation of chromatin binding / CKM complex / negative regulation of smooth muscle cell differentiation / enucleate erythrocyte development / regulation of RNA biosynthetic process / positive regulation of type II interferon-mediated signaling pathway / androgen biosynthetic process / positive regulation of G0 to G1 transition ...positive regulation of mediator complex assembly / positive regulation of T cell extravasation / positive regulation of chromatin binding / CKM complex / negative regulation of smooth muscle cell differentiation / enucleate erythrocyte development / regulation of RNA biosynthetic process / positive regulation of type II interferon-mediated signaling pathway / androgen biosynthetic process / positive regulation of G0 to G1 transition / retinal pigment epithelium development / G0 to G1 transition / mammary gland branching involved in thelarche / thyroid hormone receptor signaling pathway / core mediator complex / regulation of vitamin D receptor signaling pathway / nuclear retinoic acid receptor binding / positive regulation of hepatocyte proliferation / ventricular trabecula myocardium morphogenesis / mediator complex / positive regulation of keratinocyte differentiation / thyroid hormone generation / Generic Transcription Pathway / peroxisome proliferator activated receptor binding / embryonic heart tube development / cellular response to thyroid hormone stimulus / nuclear vitamin D receptor binding / embryonic hindlimb morphogenesis / nuclear thyroid hormone receptor binding / lens development in camera-type eye / limb development / embryonic hemopoiesis / triglyceride homeostasis / megakaryocyte development / cellular response to hepatocyte growth factor stimulus / cellular response to steroid hormone stimulus / cortical actin cytoskeleton / positive regulation of intracellular estrogen receptor signaling pathway / histone acetyltransferase binding / negative regulation of neuron differentiation / LBD domain binding / epithelial cell proliferation involved in mammary gland duct elongation / RSV-host interactions / erythrocyte development / fat cell differentiation / mammary gland branching involved in pregnancy / monocyte differentiation / skeletal muscle cell differentiation / general transcription initiation factor binding / blastocyst development / somatic stem cell population maintenance / animal organ regeneration / hematopoietic stem cell differentiation / negative regulation of keratinocyte proliferation / ubiquitin ligase complex / positive regulation of transcription initiation by RNA polymerase II / embryonic placenta development / nuclear receptor-mediated steroid hormone signaling pathway / nuclear retinoid X receptor binding / negative regulation of fibroblast proliferation / RNA polymerase II preinitiation complex assembly / keratinocyte differentiation / : / lactation / Regulation of lipid metabolism by PPARalpha / peroxisome proliferator activated receptor signaling pathway / BMAL1:CLOCK,NPAS2 activates circadian expression / Activation of gene expression by SREBF (SREBP) / cellular response to epidermal growth factor stimulus / positive regulation of erythrocyte differentiation / cholesterol homeostasis / nuclear estrogen receptor binding / nuclear receptor binding / transcription coregulator activity / transcription initiation at RNA polymerase II promoter / chromatin DNA binding / mRNA transcription by RNA polymerase II / promoter-specific chromatin binding / positive regulation of transcription elongation by RNA polymerase II / liver development / Heme signaling / Transcriptional activation of mitochondrial biogenesis / PPARA activates gene expression / protein-DNA complex / Cytoprotection by HMOX1 / brain development / Transcriptional regulation of white adipocyte differentiation / Nuclear Receptor transcription pathway / transcription coactivator binding / cell morphogenesis / : / protein import into nucleus / DNA-directed RNA polymerase activity / ubiquitin protein ligase activity / transcription corepressor activity / actin binding / MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesis and hepatic steatosis / angiogenesis / transcription regulator complex / DNA-binding transcription factor binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 4.66 Å | ||||||
![]() | Zhao, H. / Asturias, F. | ||||||
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![]() | ![]() Title: 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. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.3 MB | Display | ![]() |
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PDB format | ![]() | 955.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.5 MB | Display | ![]() |
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Full document | ![]() | 1.6 MB | Display | |
Data in XML | ![]() | 190.9 KB | Display | |
Data in CIF | ![]() | 308.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-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 ![]() |
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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 ... , 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) ![]() |
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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: ![]() |
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: ![]() |
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 |