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7ENC

TFIID-based PIC-Mediator holo-complex in fully-assembled state (hPIC-MED)

This is a non-PDB format compatible entry.
Summary for 7ENC
Entry DOI10.2210/pdb7enc/pdb
EMDB information31207
DescriptorMediator of RNA polymerase II transcription subunit 1, Mediator of RNA polymerase II transcription subunit 11, Mediator of RNA polymerase II transcription subunit 14, ... (73 entities in total)
Functional Keywordsmediator, preinitiation complex, transcription initiation, transcription
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains76
Total formula weight3882036.83
Authors
Chen, X.,Qi, Y.,Wang, X.,Wu, Z.,Yin, X.,Li, J.,Liu, W.,Xu, Y. (deposition date: 2021-04-16, release date: 2021-05-26, Last modification date: 2024-10-16)
Primary citationChen, X.,Yin, X.,Li, J.,Wu, Z.,Qi, Y.,Wang, X.,Liu, W.,Xu, Y.
Structures of the human Mediator and Mediator-bound preinitiation complex.
Science, 372:-, 2021
Cited by
PubMed Abstract: The 1.3-megadalton transcription factor IID (TFIID) is required for preinitiation complex (PIC) assembly and RNA polymerase II (Pol II)-mediated transcription initiation on almost all genes. The 26-subunit Mediator stimulates transcription and cyclin-dependent kinase 7 (CDK7)-mediated phosphorylation of the Pol II C-terminal domain (CTD). We determined the structures of human Mediator in the Tail module-extended (at near-atomic resolution) and Tail-bent conformations and structures of TFIID-based PIC-Mediator (76 polypeptides, ~4.1 megadaltons) in four distinct conformations. PIC-Mediator assembly induces concerted reorganization (Head-tilting and Middle-down) of Mediator and creates a Head-Middle sandwich, which stabilizes two CTD segments and brings CTD to CDK7 for phosphorylation; this suggests a CTD-gating mechanism favorable for phosphorylation. The TFIID-based PIC architecture modulates Mediator organization and TFIIH stabilization, underscoring the importance of TFIID in orchestrating PIC-Mediator assembly.
PubMed: 33958484
DOI: 10.1126/science.abg0635
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.13 Å)
Structure validation

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