5FZ5
Transcription initiation complex structures elucidate DNA opening (CC)
Summary for 5FZ5
Entry DOI | 10.2210/pdb5fz5/pdb |
Related | 5FYW |
EMDB information | 3383 |
Descriptor | DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB1, DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC 5, DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB11, ... (24 entities in total) |
Functional Keywords | transcription, gene expression, transcription initiation |
Biological source | SACCHAROMYCES CEREVISIAE (BAKER'S YEAST) More |
Total number of polymer chains | 22 |
Total formula weight | 890127.28 |
Authors | Plaschka, C.,Hantsche, M.,Dienemann, C.,Burzinski, C.,Plitzko, J.,Cramer, P. (deposition date: 2016-03-10, release date: 2016-05-18, Last modification date: 2024-05-08) |
Primary citation | Plaschka, C.,Hantsche, M.,Dienemann, C.,Burzinski, C.,Plitzko, J.,Cramer, P. Transcription Initiation Complex Structures Elucidate DNA Opening Nature, 533:353-, 2016 Cited by PubMed Abstract: Transcription of eukaryotic protein-coding genes begins with assembly of the RNA polymerase (Pol) II initiation complex and promoter DNA opening. Here we report cryo-electron microscopy (cryo-EM) structures of yeast initiation complexes containing closed and open DNA at resolutions of 8.8 Å and 3.6 Å, respectively. DNA is positioned and retained over the Pol II cleft by a network of interactions between the TATA-box-binding protein TBP and transcription factors TFIIA, TFIIB, TFIIE, and TFIIF. DNA opening occurs around the tip of the Pol II clamp and the TFIIE 'extended winged helix' domain, and can occur in the absence of TFIIH. Loading of the DNA template strand into the active centre may be facilitated by movements of obstructing protein elements triggered by allosteric binding of the TFIIE 'E-ribbon' domain. The results suggest a unified model for transcription initiation with a key event, the trapping of open promoter DNA by extended protein-protein and protein-DNA contacts. PubMed: 27193681DOI: 10.1038/NATURE17990 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (8.8 Å) |
Structure validation
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