2P4V

Crystal structure of the transcript cleavage factor, GreB at 2.6A resolution

2P4V の概要

• エントリーDOI: 10.2210/pdb2p4v/pdb
• 関連するPDBエントリー: 1GRJ 2ETN 2EUL 2F23
• 分子名称: Transcription elongation factor greB (2 entities in total)
• 機能のキーワード: transcription, transcript cleavage, gre-factors, rna polymerase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 111438.65

構造登録者

Vassylyeva, M.N.,Svetlov, V.,Dearborn, A.D.,Klyuyev, S.,Artsimovitch, I.,Vassylyev, D.G. (登録日: 2007-03-13, 公開日: 2008-01-22, 最終更新日: 2024-02-21)

主引用文献

Vassylyeva, M.N.,Svetlov, V.,Dearborn, A.D.,Klyuyev, S.,Artsimovitch, I.,Vassylyev, D.G.
The carboxy-terminal coiled-coil of the RNA polymerase beta'-subunit is the main binding site for Gre factors.
Embo Rep., 8:1038-1043, 2007

PubMed Abstract: Bacterial Gre transcript cleavage factors stimulate the intrinsic endonucleolytic activity of RNA polymerase (RNAP) to rescue stalled transcription complexes. They bind to RNAP and extend their coiled-coil (CC) domains to the catalytic centre through the secondary channel. Three existing models for the Gre-RNAP complex postulate congruent mechanisms of Gre-assisted catalysis, while offering conflicting views of the Gre-RNAP interactions. Here, we report the GreB structure of Escherichia coli. The GreB monomers form a triangle with the tip of the amino-terminal CC of one molecule trapped within the hydrophobic cavity of the carboxy-terminal domain of a second molecule. This arrangement suggests an analogous model for recruitment to RNAP. Indeed, the beta'-subunit CC located at the rim of the secondary channel has conserved hydrophobic residues at its tip. We show that substitutions of these residues and those in the GreB C-terminal domain cavity confer defects in GreB activity and binding to RNAP, and present a plausible model for the RNAP-GreB complex.

PubMed: 17917675
DOI: 10.1038/sj.embor.7401079

実験手法

X-RAY DIFFRACTION (2.6 Å)