6HQA
Molecular structure of promoter-bound yeast TFIID
Summary for 6HQA
| Entry DOI | 10.2210/pdb6hqa/pdb |
| EMDB information | 0251 |
| Descriptor | Taf2, Subunit (90 kDa) of TFIID and SAGA complexes, Subunit (60 kDa) of TFIID and SAGA complexes, ... (9 entities in total) |
| Functional Keywords | complex, transcription initiation, transcription |
| Biological source | Komagataella phaffii GS115 More |
| Total number of polymer chains | 11 |
| Total formula weight | 634429.33 |
| Authors | Kolesnikova, O.,Ben-Shem, A.,Luo, J.,Ranish, J.,Schultz, P.,Papai, G. (deposition date: 2018-09-24, release date: 2018-11-21, Last modification date: 2024-10-23) |
| Primary citation | Kolesnikova, O.,Ben-Shem, A.,Luo, J.,Ranish, J.,Schultz, P.,Papai, G. Molecular structure of promoter-bound yeast TFIID. Nat Commun, 9:4666-4666, 2018 Cited by PubMed 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. PubMed: 30405110DOI: 10.1038/s41467-018-07096-y PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (7.1 Å) |
Structure validation
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