5IYD

Human core-PIC in the initial transcribing state (no IIS)

Summary for 5IYD

• Entry DOI: 10.2210/pdb5iyd/pdb
• Related: 5IVW 5IY6 5IY7 5IY8 5IY9 5IYA 5IYB 5IYC
• EMDB information: 3307 8131 8132 8133 8134 8135 8136 8137 8138
• Descriptor: DNA-directed RNA polymerase II subunit RPB1, DNA-directed RNA polymerase II subunit RPB10, DNA-directed RNA polymerase II subunit RPB11-a, ... (25 entities in total)
• Functional Keywords: initiation, rna polymerase ii, human, transcription, transferase-dna-rna complex, transferase/dna/rna
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 23
• Total formula weight: 865366.64

Authors

He, Y.,Yan, C.,Fang, J.,Inouye, C.,Tjian, R.,Ivanov, I.,Nogales, E. (deposition date: 2016-03-24, release date: 2016-05-18, Last modification date: 2019-11-20)

Primary citation

He, Y.,Yan, C.,Fang, J.,Inouye, C.,Tjian, R.,Ivanov, I.,Nogales, E.
Near-atomic resolution visualization of human transcription promoter opening.
Nature, 533:359-365, 2016

PubMed Abstract: In eukaryotic transcription initiation, a large multi-subunit pre-initiation complex (PIC) that assembles at the core promoter is required for the opening of the duplex DNA and identification of the start site for transcription by RNA polymerase II. Here we use cryo-electron microscropy (cryo-EM) to determine near-atomic resolution structures of the human PIC in a closed state (engaged with duplex DNA), an open state (engaged with a transcription bubble), and an initially transcribing complex (containing six base pairs of DNA-RNA hybrid). Our studies provide structures for previously uncharacterized components of the PIC, such as TFIIE and TFIIH, and segments of TFIIA, TFIIB and TFIIF. Comparison of the different structures reveals the sequential conformational changes that accompany the transition from each state to the next throughout the transcription initiation process. This analysis illustrates the key role of TFIIB in transcription bubble stabilization and provides strong structural support for a translocase activity of XPB.

PubMed: 27193682
DOI: 10.1038/nature17970

Experimental method

ELECTRON MICROSCOPY (3.9 Å)