5IP7

Structure of RNA Polymerase II-Tfg1 peptide complex

Summary for 5IP7

• Entry DOI: 10.2210/pdb5ip7/pdb
• Descriptor: DNA-directed RNA polymerase II subunit RPB1, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerase II subunit RPB11, ... (15 entities in total)
• Functional Keywords: transcription
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Nucleus: P04050 P38902 P08518 P16370 P20433 P20434 P34087 P20436; Nucleus, nucleolus : P22139 P40422 P27999; Cytoplasm : P20435
• Total number of polymer chains: 13
• Total formula weight: 498983.40

Authors

Plaschka, C.,Hantsche, M.,Dienemann, C.,Burzinski, C.,Plitzko, J.,Cramer, P. (deposition date: 2016-03-09, release date: 2016-05-11, Last modification date: 2024-01-10)

Primary citation

Plaschka, C.,Hantsche, M.,Dienemann, C.,Burzinski, C.,Plitzko, J.,Cramer, P.
Transcription initiation complex structures elucidate DNA opening.
Nature, 533:353-358, 2016

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: 27193681
DOI: 10.1038/nature17990

Experimental method

X-RAY DIFFRACTION (3.52 Å)