EMD-0255

Single-particle
4.8 Å
EMD-0255 Deposition: 25/09/2018
Map released: 21/11/2018
Last modified: 25/11/2020
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-0255

Molecular structure of promoter-bound yeast TFIID (locally-refined Twin lobe)

EMD-0255

Single-particle
4.8 Å
EMD-0255 Deposition: 25/09/2018
Map released: 21/11/2018
Last modified: 25/11/2020
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Komagataella phaffii GS115
Sample: Transcription Factor IID

Deposition Authors: Kolesnikova O, Ben-Shem A, Luo J, Ranish J, Schultz P, Papai G
Molecular structure of promoter-bound yeast TFIID.
Kolesnikova O , Ben-Shem A , Luo J , Ranish J , Schultz P , Papai G
(2018) Nat Commun , 9 , 4666 - 4666
PUBMED: 30405110
DOI: doi:10.1038/s41467-018-07096-y
ISSN: 2041-1723
Abstract:
Transcription preinitiation complex assembly on the promoters of protein encoding genes is nucleated in vivo by TFIID composed of the TATA-box Binding Protein (TBP) and 13 TBP-associate factors (Tafs) providing regulatory and chromatin binding functions. Here we present the cryo-electron microscopy structure of promoter-bound yeast TFIID at a resolution better than 5 Å, except for a flexible domain. We position the crystal structures of several subunits and, in combination with cross-linking studies, describe the quaternary organization of TFIID. The compact tri lobed architecture is stabilized by a topologically closed Taf5-Taf6 tetramer. We confirm the unique subunit stoichiometry prevailing in TFIID and uncover a hexameric arrangement of Tafs containing a histone fold domain in the Twin lobe.