2N9U

Solution NMR structure of Erythrobacter litoralis PhyR response regulator REC domain

2N9U の概要

• エントリーDOI: 10.2210/pdb2n9u/pdb
• NMR情報: BMRB: 25918
• 分子名称: Response regulator (1 entity in total)
• 機能のキーワード: response regulator, receiver, two-component signaling, transcription
• 由来する生物種: Erythrobacter litoralis HTCC2594
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13823.53

構造登録者

Correa, F.,Gardner, K.H. (登録日: 2015-12-09, 公開日: 2016-09-07, 最終更新日: 2024-05-15)

主引用文献

Correa, F.,Gardner, K.H.
Basis of Mutual Domain Inhibition in a Bacterial Response Regulator.
Cell Chem Biol, 23:945-954, 2016

PubMed Abstract: Information transmission in biological signaling networks is commonly considered to be a unidirectional flow of information between protein partners. According to this view, many bacterial response regulator proteins utilize input receiver (REC) domains to "switch" functional outputs, using REC phosphorylation to shift pre-existing equilibria between inactive and active conformations. However, recent data indicate that output domains themselves also shift such equilibria, implying a "mutual inhibition" model. Here we use solution nuclear magnetic resonance to provide a mechanistic basis for such control in a PhyR-type response regulator. Our structure of the isolated, non-phosphorylated REC domain surprisingly reveals a fully active conformation, letting us identify structural and dynamic changes imparted by the output domain to inactivate the full-length protein. Additional data reveal transient structural changes within the full-length protein, facilitating activation. Our data provide a basis for understanding the changes that REC and output domains undergo to set a default "inactive" state.

PubMed: 27524295
DOI: 10.1016/j.chembiol.2016.07.010

実験手法

SOLUTION NMR