1Y1V

Refined RNA Polymerase II-TFIIS complex

1Y1V の概要

• エントリーDOI: 10.2210/pdb1y1v/pdb
• 関連するPDBエントリー: 1PQV
• 分子名称: DNA-directed RNA polymerase II largest subunit, DNA-directed RNA polymerases I/II/III subunit 10, DNA-directed RNA polymerase II 13.6 kDa polypeptide, ... (15 entities in total)
• 機能のキーワード: rna polymerase ii, tfiis, transcription, elongation, transferase-transcription complex, transferase/transcription
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• タンパク質・核酸の鎖数: 13
• 化学式量合計: 535043.15

構造登録者

Kettenberger, H.,Armache, K.-J.,Cramer, P. (登録日: 2004-11-19, 公開日: 2004-12-28, 最終更新日: 2024-03-13)

主引用文献

Kettenberger, H.,Armache, K.J.,Cramer, P.
Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS.
Mol.Cell, 16:955-965, 2004

PubMed Abstract: The crystal structure of the complete 12 subunit RNA polymerase (pol) II bound to a transcription bubble and product RNA reveals incoming template and nontemplate DNA, a seven base pair DNA/RNA hybrid, and three nucleotides each of separating DNA and RNA. The complex adopts the posttranslocation state and accommodates a cocrystallized nucleoside triphosphate (NTP) substrate. The NTP binds in the active site pore at a position to interact with a DNA template base. Residues surrounding the NTP are conserved in all cellular RNA polymerases, suggesting a universal mechanism of NTP selection and incorporation. DNA-DNA and DNA-RNA strand separation may be explained by pol II-induced duplex distortions. Four protein loops partition the active center cleft, contribute to embedding the hybrid, prevent strand reassociation, and create an RNA exit tunnel. Binding of the elongation factor TFIIS realigns RNA in the active center, possibly converting the elongation complex to an alternative state less prone to stalling.

PubMed: 15610738
DOI: 10.1016/j.molcel.2004.11.040

実験手法

X-RAY DIFFRACTION (3.8 Å)