2MSK

Solution Structure and Chemical Shift Assignments for BeF3 activated Receiver Domain of Nitrogen Regulatory Protein C (NtrC) at 35C

Summary for 2MSK

• Entry DOI: 10.2210/pdb2msk/pdb
• Related: 2MSL
• NMR Information: BMRB: 25124
• Descriptor: Nitrogen regulation protein NR(I) (1 entity in total)
• Functional Keywords: transcription
• Biological source: Salmonella typhimurium
• Total number of polymer chains: 1
• Total formula weight: 13636.60

Authors

Clarkson, M.W.,Pontiggia, F.,Villali, J.,Kern, D. (deposition date: 2014-08-04, release date: 2015-07-01, Last modification date: 2024-05-15)

Primary citation

Pontiggia, F.,Pachov, D.V.,Clarkson, M.W.,Villali, J.,Hagan, M.F.,Pande, V.S.,Kern, D.
Free energy landscape of activation in a signalling protein at atomic resolution.
Nat Commun, 6:7284-7284, 2015

PubMed Abstract: The interconversion between inactive and active protein states, traditionally described by two static structures, is at the heart of signalling. However, how folded states interconvert is largely unknown due to the inability to experimentally observe transition pathways. Here we explore the free energy landscape of the bacterial response regulator NtrC by combining computation and nuclear magnetic resonance, and discover unexpected features underlying efficient signalling. We find that functional states are defined purely in kinetic and not structural terms. The need of a well-defined conformer, crucial to the active state, is absent in the inactive state, which comprises a heterogeneous collection of conformers. The transition between active and inactive states occurs through multiple pathways, facilitated by a number of nonnative transient hydrogen bonds, thus lowering the transition barrier through both entropic and enthalpic contributions. These findings may represent general features for functional conformational transitions within the folded state.

PubMed: 26073309
DOI: 10.1038/ncomms8284

Experimental method

SOLUTION NMR