6MZM
Human TFIID bound to promoter DNA and TFIIA
Summary for 6MZM
Entry DOI | 10.2210/pdb6mzm/pdb |
EMDB information | 9298 9299 9300 9301 9302 9305 9306 |
Descriptor | Transcription initiation factor TFIID subunit 1, TAF1, Transcription initiation factor TFIID subunit 10, Transcription initiation factor TFIID subunit 12, ... (17 entities in total) |
Functional Keywords | transcription, dna, nuclear, transcription-dna complex, transcription/dna |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 17 |
Total formula weight | 800424.26 |
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: 2024-03-13) |
Primary citation | Patel, 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: 30442764DOI: 10.1126/science.aau8872 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (7.5 Å) |
Structure validation
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