2OUG

Crystal structure of the RfaH transcription factor at 2.1A resolution

2OUG の概要

• エントリーDOI: 10.2210/pdb2oug/pdb
• 分子名称: Transcriptional activator rfaH (2 entities in total)
• 機能のキーワード: transcription factor, virulence, transcription pausing, transcription elongation, transcription
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 73456.87

構造登録者

Vassylyev, D.G.,Vassylyeva, M.N.,Svetlov, V.,Artsimovitch, I. (登録日: 2007-02-10, 公開日: 2007-05-01, 最終更新日: 2024-02-21)

主引用文献

Belogurov, G.A.,Vassylyeva, M.N.,Svetlov, V.,Klyuyev, S.,Grishin, N.V.,Vassylyev, D.G.,Artsimovitch, I.
Structural basis for converting a general transcription factor into an operon-specific virulence regulator.
Mol.Cell, 26:117-129, 2007

PubMed Abstract: RfaH, a paralog of the general transcription factor NusG, is recruited to elongating RNA polymerase at specific regulatory sites. The X-ray structure of Escherichia coli RfaH reported here reveals two domains. The N-terminal domain displays high similarity to that of NusG. In contrast, the alpha-helical coiled-coil C domain, while retaining sequence similarity, is strikingly different from the beta barrel of NusG. To our knowledge, such an all-beta to all-alpha transition of the entire domain is the most extreme example of protein fold evolution known to date. Both N domains possess a vast hydrophobic cavity that is buried by the C domain in RfaH but is exposed in NusG. We propose that this cavity constitutes the RNA polymerase-binding site, which becomes unmasked in RfaH only upon sequence-specific binding to the nontemplate DNA strand that triggers domain dissociation. Finally, we argue that RfaH binds to the beta' subunit coiled coil, the major target site for the initiation sigma factors.

PubMed: 17434131
DOI: 10.1016/j.molcel.2007.02.021

実験手法

X-RAY DIFFRACTION (2.1 Å)