Free energy landscape of activation in a signalling protein at atomic resolution.

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 pat

SUBMITTER: Pontiggia F 

PROVIDER: S-EPMC4470301 | biostudies-literature | 2015 Jun

REPOSITORIES: biostudies-literature