Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6MZL

Human TFIID canonical state

Summary for 6MZL
Entry DOI10.2210/pdb6mzl/pdb
EMDB information9298 9299 9300 9301 9302 9305 9306
DescriptorTranscription initiation factor TFIID subunit 1, Transcription initiation factor TFIID subunit 9, TAF9, Transcription initiation factor TFIID subunit 10, ... (17 entities in total)
Functional Keywordstranscription, dna, nuclear
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains22
Total formula weight1305174.06
Authors
Patel, A.B.,Louder, R.K.,Greber, B.J.,Grunberg, S.,Luo, J.,Fang, J.,Liu, Y.,Ranish, J.,Hahn, S.,Nogales, E. (deposition date: 2018-11-05, release date: 2018-11-28, Last modification date: 2019-11-20)
Primary citationPatel, A.B.,Louder, R.K.,Greber, B.J.,Grunberg, S.,Luo, J.,Fang, J.,Liu, Y.,Ranish, J.,Hahn, S.,Nogales, E.
Structure of human TFIID and mechanism of TBP loading onto promoter DNA.
Science, 362:-, 2018
Cited by
PubMed Abstract: The general transcription factor IID (TFIID) is a critical component of the eukaryotic transcription preinitiation complex (PIC) and is responsible for recognizing the core promoter DNA and initiating PIC assembly. We used cryo-electron microscopy, chemical cross-linking mass spectrometry, and biochemical reconstitution to determine the complete molecular architecture of TFIID and define the conformational landscape of TFIID in the process of TATA box-binding protein (TBP) loading onto promoter DNA. Our structural analysis revealed five structural states of TFIID in the presence of TFIIA and promoter DNA, showing that the initial binding of TFIID to the downstream promoter positions the upstream DNA and facilitates scanning of TBP for a TATA box and the subsequent engagement of the promoter. Our findings provide a mechanistic model for the specific loading of TBP by TFIID onto the promoter.
PubMed: 30442764
DOI: 10.1126/science.aau8872
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (23 Å)
Structure validation

226707

數據於2024-10-30公開中

PDB statisticsPDBj update infoContact PDBjnumon