Tuning site-specific dynamics to drive allosteric activation in a pneumococcal zinc uptake regulator.

ABSTRACT: MarR (multiple antibiotic resistance repressor) family proteins are bacterial repressors that regulate transcription in response to a wide range of chemical signals. Although specific features of MarR family function have been described, the role of atomic motions in MarRs remains unexplored thus limiting insights into the evolution of allostery in this ubiquitous family of repressors. Here, we provide the first experimental evidence that internal dynamics play a crucial functional role in MarR proteins. Streptococcus pneumoniae AdcR (adhesin-competence repressor) regulates Zn^II homeostasis and Zn^II functions as an allosteric activator of DNA binding. Zn^II coordination triggers a transition from somewhat independent domains to a more compact structur

SUBMITTER: Capdevila DA 

PROVIDER: S-EPMC6224198 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature