3K1F

Crystal structure of RNA Polymerase II in complex with TFIIB

3K1F の概要

• エントリーDOI: 10.2210/pdb3k1f/pdb
• 分子名称: DNA-directed RNA polymerase II subunit RPB1, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerase II subunit RPB11, ... (14 entities in total)
• 機能のキーワード: rna polymerase ii, tfiib, transcription factor, transcription initiation, dna-binding, dna-directed rna polymerase, isopeptide bond, magnesium, metal-binding, nucleotidyltransferase, nucleus, phosphoprotein, transcription, transferase, zinc-finger, dna damage, dna repair, mrna processing, initiation factor
• 由来する生物種: Saccharomyces cerevisiae (yeast); 詳細
• 細胞内の位置: Nucleus: P04050 P38902 P08518 P16370 P20433 P20434 P34087 P20436 P27999; Nucleus, nucleolus: P22139 P40422; Cytoplasm: P20435
• タンパク質・核酸の鎖数: 13
• 化学式量合計: 533438.36

構造登録者

Kostrewa, D.,Zeller, M.E.,Armache, K.-J.,Seizl, M.,Leike, K.,Thomm, M.,Cramer, P. (登録日: 2009-09-27, 公開日: 2009-11-10, 最終更新日: 2023-09-06)

主引用文献

Kostrewa, D.,Zeller, M.E.,Armache, K.J.,Seizl, M.,Leike, K.,Thomm, M.,Cramer, P.
RNA polymerase II-TFIIB structure and mechanism of transcription initiation.
Nature, 462:323-330, 2009

PubMed Abstract: To initiate gene transcription, RNA polymerase II (Pol II) requires the transcription factor IIB (B). Here we present the crystal structure of the complete Pol II-B complex at 4.3 A resolution, and complementary functional data. The results indicate the mechanism of transcription initiation, including the transition to RNA elongation. Promoter DNA is positioned over the Pol II active centre cleft with the 'B-core' domain that binds the wall at the end of the cleft. DNA is then opened with the help of the 'B-linker' that binds the Pol II rudder and clamp coiled-coil at the edge of the cleft. The DNA template strand slips into the cleft and is scanned for the transcription start site with the help of the 'B-reader' that approaches the active site. Synthesis of the RNA chain and rewinding of upstream DNA displace the B-reader and B-linker, respectively, to trigger B release and elongation complex formation.

PubMed: 19820686
DOI: 10.1038/nature08548

実験手法

X-RAY DIFFRACTION (4.3 Å)