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7ML3

General transcription factor TFIIH (weak binding)

Summary for 7ML3
Entry DOI10.2210/pdb7ml3/pdb
EMDB information23904 23905 23906 23907 23908
DescriptorBJ4_G0050160.mRNA.1.CDS.1, template strand DNA, ZINC ION, ... (12 entities in total)
Functional Keywordspic, tfiih, transcription, itc, rna polymerase ii
Biological sourceSaccharomyces cerevisiae (Baker's yeast)
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Total number of polymer chains10
Total formula weight457270.24
Authors
Yang, C.,Fujiwara, R.,Kim, H.J.,Gorbea Colon, J.J.,Steimle, S.,Garcia, B.A.,Murakami, K. (deposition date: 2021-04-27, release date: 2022-02-02, Last modification date: 2022-02-16)
Primary citationYang, C.,Fujiwara, R.,Kim, H.J.,Basnet, P.,Zhu, Y.,Gorbea Colon, J.J.,Steimle, S.,Garcia, B.A.,Kaplan, C.D.,Murakami, K.
Structural visualization of de novo transcription initiation by Saccharomyces cerevisiae RNA polymerase II.
Mol.Cell, 82:660-676.e9, 2022
Cited by
PubMed Abstract: Previous structural studies of the initiation-elongation transition of RNA polymerase II (pol II) transcription have relied on the use of synthetic oligonucleotides, often artificially discontinuous to capture pol II in the initiating state. Here, we report multiple structures of initiation complexes converted de novo from a 33-subunit yeast pre-initiation complex (PIC) through catalytic activities and subsequently stalled at different template positions. We determine that PICs in the initially transcribing complex (ITC) can synthesize a transcript of ∼26 nucleotides before transitioning to an elongation complex (EC) as determined by the loss of general transcription factors (GTFs). Unexpectedly, transition to an EC was greatly accelerated when an ITC encountered a downstream EC stalled at promoter proximal regions and resulted in a collided head-to-end dimeric EC complex. Our structural analysis reveals a dynamic state of TFIIH, the largest of GTFs, in PIC/ITC with distinct functional consequences at multiple steps on the pathway to elongation.
PubMed: 35051353
DOI: 10.1016/j.molcel.2021.12.020
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (7.6 Å)
Structure validation

226707

数据于2024-10-30公开中

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