2N9U

Solution NMR structure of Erythrobacter litoralis PhyR response regulator REC domain

Summary for 2N9U

• Entry DOI: 10.2210/pdb2n9u/pdb
• NMR Information: BMRB: 25918
• Descriptor: Response regulator (1 entity in total)
• Functional Keywords: response regulator, receiver, two-component signaling, transcription
• Biological source: Erythrobacter litoralis HTCC2594
• Total number of polymer chains: 1
• Total formula weight: 13823.53

Authors

Correa, F.,Gardner, K.H. (deposition date: 2015-12-09, release date: 2016-09-07, Last modification date: 2024-05-15)

Primary citation

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

Experimental method

SOLUTION NMR