4LRY

Crystal Structure of the E.coli DhaR(N)-DhaK(T79L) complex

4LRY の概要

• エントリーDOI: 10.2210/pdb4lry/pdb
• 関連するPDBエントリー: 4LRX 4LRZ
• 分子名称: PTS-dependent dihydroxyacetone kinase, dihydroxyacetone-binding subunit DhaK, PTS-dependent dihydroxyacetone kinase operon regulatory protein, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: coiled-coil, helix rotation, gaf, pas, transcriptional regulation complex, transferase-transcription regulator complex, transferase/transcription regulator
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 146490.19

構造登録者

Shi, R.,McDonald, L.,Cygler, M.,Ekiel, I. (登録日: 2013-07-21, 公開日: 2014-01-29, 最終更新日: 2024-02-28)

主引用文献

Shi, R.,McDonald, L.,Cygler, M.,Ekiel, I.
Coiled-Coil Helix Rotation Selects Repressing or Activating State of Transcriptional Regulator DhaR.
Structure, 22:478-487, 2014

PubMed Abstract: Escherichia coli dihydroxyacetone (Dha) kinase consists of two subunits, DhaK and DhaL. Transcription of dha operon is regulated by the DhaR transcription factor and its action is under control of the kinase subunits. DhaR is activated by interaction with DhaL while it is repressed by DhaK. We have determined the structures of DhaK and DhaL bound to the tandem GAF-like and PAS domains of the DhaR, providing an architectural model for how GAF/PAS tandem domains work together in binding protein partners. The structures reveal a mechanism of opposite transcriptional regulation by the DhaK and DhaL subunits. The kinase subunits interface with DhaR through surfaces that partially overlap with their active sites, allowing sensing of ATP- versus ADP-loaded DhaL subunit and also precluding a ternary complex between DhaK-DhaL and DhaR. The rotation of helices within the DhaR coiled-coil linker upon DhaL binding provides the mechanism for transmitting the binding signal from the GAF/PAS domains to the C-terminal DNA-binding domain.

PubMed: 24440518
DOI: 10.1016/j.str.2013.11.012

実験手法

X-RAY DIFFRACTION (2.83 Å)