Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

7EG7

TFIID-based core PIC on SCP promoter

Summary for 7EG7
Entry DOI10.2210/pdb7eg7/pdb
EMDB information31107
DescriptorTranscription initiation factor TFIID subunit 1, Transcription initiation factor TFIID subunit 12, Transcription initiation factor IIA subunit 2, ... (35 entities in total)
Functional Keywordstfiid, preinitiation complex, core promoter, transcription initiation, transcription
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains39
Total formula weight2023435.80
Authors
Chen, X.,Qi, Y.,Hou, H.,Wang, X.,Wu, Z.,Li, J.,Xu, Y. (deposition date: 2021-03-24, release date: 2021-05-05, Last modification date: 2024-10-09)
Primary citationChen, X.,Qi, Y.,Wu, Z.,Wang, X.,Li, J.,Zhao, D.,Hou, H.,Li, Y.,Yu, Z.,Liu, W.,Wang, M.,Ren, Y.,Li, Z.,Yang, H.,Xu, Y.
Structural insights into preinitiation complex assembly on core promoters.
Science, 372:-, 2021
Cited by
PubMed Abstract: Transcription factor IID (TFIID) recognizes core promoters and supports preinitiation complex (PIC) assembly for RNA polymerase II (Pol II)-mediated eukaryotic transcription. We determined the structures of human TFIID-based PIC in three stepwise assembly states and revealed two-track PIC assembly: stepwise promoter deposition to Pol II and extensive modular reorganization on track I (on TATA-TFIID-binding element promoters) versus direct promoter deposition on track II (on TATA-only and TATA-less promoters). The two tracks converge at an ~50-subunit holo PIC in identical conformation, whereby TFIID stabilizes PIC organization and supports loading of cyclin-dependent kinase (CDK)-activating kinase (CAK) onto Pol II and CAK-mediated phosphorylation of the Pol II carboxyl-terminal domain. Unexpectedly, TBP of TFIID similarly bends TATA box and TATA-less promoters in PIC. Our study provides structural visualization of stepwise PIC assembly on highly diversified promoters.
PubMed: 33795473
DOI: 10.1126/science.aba8490
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (6.2 Å)
Structure validation

229183

PDB entries from 2024-12-18

PDB statisticsPDBj update infoContact PDBjnumon