Protein plasticity driven by disorder and collapse governs the heterogeneous binding of CytR to DNA.

ABSTRACT: The amplitude of thermodynamic fluctuations in biological macromolecules determines their conformational behavior, dimensions, nature of phase transitions and effectively their specificity and affinity, thus contributing to fine-tuned molecular recognition. Unique among large-scale conformational changes in proteins are temperature-induced collapse transitions in intrinsically disordered proteins (IDPs). Here, we show that CytR DNA-binding domain, an IDP that folds on binding DNA, undergoes a coil-to-globule transition with temperature in the absence of DNA while exhibiting energetically decoupled local and global structural rearrangements, and maximal thermodynamic fluctuations at the optimal bacterial growth temperature. The collapse is shown to be a continuous transition through a combi

SUBMITTER: Munshi S 

PROVIDER: S-EPMC5934615 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature