5FUR
Structure of human TFIID-IIA bound to core promoter DNA
Summary for 5FUR
Entry DOI | 10.2210/pdb5fur/pdb |
EMDB information | 3305 |
Descriptor | TATA-BOX-BINDING PROTEIN, TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 6, TRANSCRIPTION INITIATION FACTOR TFIID SUBUNIT 8, ... (11 entities in total) |
Functional Keywords | tfiid, tfiia, transcription, rna polymerase ii, general transcription factors, preinitiation complex, core promoter, dna binding |
Biological source | HOMO SAPIENS (HUMAN) More |
Cellular location | Nucleus : P20226 P49848 Q7Z7C8 P52655 P52655 P52657 P21675 Q15545 Q6P1X5 |
Total number of polymer chains | 12 |
Total formula weight | 688289.19 |
Authors | Louder, R.K.,He, Y.,Lopez-Blanco, J.R.,Fang, J.,Chacon, P.,Nogales, E. (deposition date: 2016-01-29, release date: 2016-04-06, Last modification date: 2024-11-13) |
Primary citation | Louder, R.K.,He, Y.,Lopez-Blanco, J.R.,Fang, J.,Chacon, P.,Nogales, E. Structure of Promoter-Bound TFIID and Model of Human Pre-Initiation Complex Assembly. Nature, 531:604-, 2016 Cited by PubMed Abstract: The general transcription factor IID (TFIID) plays a central role in the initiation of RNA polymerase II (Pol II)-dependent transcription by nucleating pre-initiation complex (PIC) assembly at the core promoter. TFIID comprises the TATA-binding protein (TBP) and 13 TBP-associated factors (TAF1-13), which specifically interact with a variety of core promoter DNA sequences. Here we present the structure of human TFIID in complex with TFIIA and core promoter DNA, determined by single-particle cryo-electron microscopy at sub-nanometre resolution. All core promoter elements are contacted by subunits of TFIID, with TAF1 and TAF2 mediating major interactions with the downstream promoter. TFIIA bridges the TBP-TATA complex with lobe B of TFIID. We also present the cryo-electron microscopy reconstruction of a fully assembled human TAF-less PIC. Superposition of common elements between the two structures provides novel insights into the general role of TFIID in promoter recognition, PIC assembly, and transcription initiation. PubMed: 27007846DOI: 10.1038/NATURE17394 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (8.5 Å) |
Structure validation
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