1IW7

Crystal structure of the RNA polymerase holoenzyme from Thermus thermophilus at 2.6A resolution

1IW7 の概要

• エントリーDOI: 10.2210/pdb1iw7/pdb
• 分子名称: RNA polymerase alpha subunit, RNA polymerase beta subunit, RNA polymerase omega subunit, ... (8 entities in total)
• 機能のキーワード: rna polymerase holoenzyme, riken structural genomics/proteomics initiative, rsgi, structural genomics, transferase
• 由来する生物種: Thermus thermophilus; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 865887.70

構造登録者

RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2002-04-22, 公開日: 2002-06-26, 最終更新日: 2023-10-25)

主引用文献

Vassylyev, D.G.,Sekine, S.,Laptenko, O.,Lee, J.,Vassylyeva, M.N.,Borukhov, S.,Yokoyama, S.
Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 A resolution
NATURE, 417:712-719, 2002

PubMed Abstract: In bacteria, the binding of a single protein, the initiation factor sigma, to a multi-subunit RNA polymerase core enzyme results in the formation of a holoenzyme, the active form of RNA polymerase essential for transcription initiation. Here we report the crystal structure of a bacterial RNA polymerase holoenzyme from Thermus thermophilus at 2.6 A resolution. In the structure, two amino-terminal domains of the sigma subunit form a V-shaped structure near the opening of the upstream DNA-binding channel of the active site cleft. The carboxy-terminal domain of sigma is near the outlet of the RNA-exit channel, about 57 A from the N-terminal domains. The extended linker domain forms a hairpin protruding into the active site cleft, then stretching through the RNA-exit channel to connect the N- and C-terminal domains. The holoenzyme structure provides insight into the structural organization of transcription intermediate complexes and into the mechanism of transcription initiation.

PubMed: 12000971
DOI: 10.1038/nature752

実験手法

X-RAY DIFFRACTION (2.6 Å)