3QWG

Crystal structure of EspRdelta10, C-terminal 10 amino acids deletion mutant of EspR transcription factor from Mycobacterium tuberculosis

3QWG の概要

• エントリーDOI: 10.2210/pdb3qwg/pdb
• 関連するPDBエントリー: 3QF3 3QYX
• 分子名称: ESX-1 secretion-associated regulator EspR (2 entities in total)
• 機能のキーワード: n-terminal helix-turn-helix motif, transcription factor, transcription
• 由来する生物種: Mycobacterium tuberculosis
• 細胞内の位置: Secreted: P96228
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27256.74

構造登録者

Blasco, B.,Pojer, F.,Cole, S.T. (登録日: 2011-02-28, 公開日: 2011-09-14, 最終更新日: 2023-09-13)

主引用文献

Blasco, B.,Stenta, M.,Alonso-Sarduy, L.,Dietler, G.,Peraro, M.D.,Cole, S.T.,Pojer, F.
Atypical DNA recognition mechanism used by the EspR virulence regulator of Mycobacterium tuberculosis.
Mol.Microbiol., 82:251-264, 2011

PubMed Abstract: The human pathogen Mycobacterium tuberculosis requires the ESX-1 secretion system for full virulence. EspR plays a key role in ESX-1 regulation via direct binding and transcriptional activation of the espACD operon. Here, we describe the crystal structures of EspR, a C-terminally truncated form, EspRΔ10, as well as an EspR-DNA complex. EspR forms a dimer with each monomer containing an N-terminal helix-turn-helix DNA binding motif and an atypical C-terminal dimerization domain. Structural studies combined with footprinting experiments, atomic force microscopy and molecular dynamic simulations allow us to propose a model in which a dimer of EspR dimers is the minimal functional unit with two subunits binding two consecutive major grooves. The other two DNA binding domains are thus free to form higher-order oligomers and to bridge distant DNA sites in a cooperative way. These features are reminiscent of nucleoid-associated proteins and suggest a more general regulatory role for EspR than was previously suspected.

PubMed: 21883526
DOI: 10.1111/j.1365-2958.2011.07813.x

実験手法

X-RAY DIFFRACTION (1.992 Å)