Description
Experimental Technique/Method:ELECTRON MICROSCOPY
Resolution:8.5
Classification:TRANSCRIPTION
Release Date:2016-04-06
Deposition Date:2016-01-29
Revision Date:2016-04-13#2017-08-02
Molecular Weight:688289.19
Macromolecule Type:Protein#DNA
Residue Count:5813
Atom Site Count:21485
DOI:10.2210/pdb5fur/pdb
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.
Resolution:8.5
Classification:TRANSCRIPTION
Release Date:2016-04-06
Deposition Date:2016-01-29
Revision Date:2016-04-13#2017-08-02
Molecular Weight:688289.19
Macromolecule Type:Protein#DNA
Residue Count:5813
Atom Site Count:21485
DOI:10.2210/pdb5fur/pdb
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.
| Date made available | 2016 |
|---|---|
| Publisher | RCSB-PDB |