Structural and functional basis of transcriptional regulation by TetR family protein CprB from S. coelicolor A3(2).

ABSTRACT: Antibiotic production and resistance pathways in Streptomyces are dictated by the interplay of transcriptional regulatory proteins that trigger downstream responses via binding to small diffusible molecules. To decipher the mode of DNA binding and the associated allosteric mechanism in the sub-class of transcription factors that are induced by γ-butyrolactones, we present the crystal structure of CprB in complex with the consensus DNA element to a resolution of 3.25 Å. Binding of the DNA results in the restructuring of the dimeric interface of CprB, inducing a pendulum-like motion of the helix-turn-helix motif that inserts into the major groove. The crystal structure revealed that, CprB is bound to DNA as a dimer of dimers with the mode of binding being analogous to the broad spectrum mult

SUBMITTER: Bhukya H 

PROVIDER: S-EPMC4150764 | biostudies-literature | 2014 Sep

REPOSITORIES: biostudies-literature