5M5Y

RNA Polymerase I elongation complex 2

5M5Y の概要

• エントリーDOI: 10.2210/pdb5m5y/pdb
• EMDBエントリー: 3448
• 分子名称: DNA-directed RNA polymerase I subunit RPA190, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerases I and III subunit RPAC2, ... (18 entities in total)
• 機能のキーワード: rna polymerase, 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: 17
• 化学式量合計: 637065.66

構造登録者

Tafur, L.,Sadian, Y.,Hoffmann, N.A.,Jakobi, A.J.,Wetzel, R.,Hagen, W.J.H.,Sachse, C.,Muller, C.W. (登録日: 2016-10-23, 公開日: 2016-12-21, 最終更新日: 2025-12-17)

主引用文献

Tafur, L.,Sadian, Y.,Hoffmann, N.A.,Jakobi, A.J.,Wetzel, R.,Hagen, W.J.,Sachse, C.,Muller, C.W.
Molecular Structures of Transcribing RNA Polymerase I.
Mol. Cell, 64:1135-1143, 2016

PubMed Abstract: RNA polymerase I (Pol I) is a 14-subunit enzyme that solely synthesizes pre-ribosomal RNA. Recently, the crystal structure of apo Pol I gave unprecedented insight into its molecular architecture. Here, we present three cryo-EM structures of elongating Pol I, two at 4.0 Å and one at 4.6 Å resolution, and a Pol I open complex at 3.8 Å resolution. Two modules in Pol I mediate the narrowing of the DNA-binding cleft by closing the clamp domain. The DNA is bound by the clamp head and by the protrusion domain, allowing visualization of the upstream and downstream DNA duplexes in one of the elongation complexes. During formation of the Pol I elongation complex, the bridge helix progressively folds, while the A12.2 C-terminal domain is displaced from the active site. Our results reveal the conformational changes associated with elongation complex formation and provide additional insight into the Pol I transcription cycle.

PubMed: 27867008
DOI: 10.1016/j.molcel.2016.11.013

実験手法

ELECTRON MICROSCOPY (4 Å)