Allosteric signaling in the biotin repressor occurs via local folding coupled to global dampening of protein dynamics.

ABSTRACT: The biotin repressor is an allosterically regulated, site-specific DNA-binding protein. Binding of the small ligand bio-5'-AMP activates repressor dimerization, which is a prerequisite to DNA binding. Multiple disorder-to-order transitions, some of which are known to be important for the functional allosteric response, occur in the vicinity of the ligand-binding site concomitant with effector binding to the repressor monomer. In this work, the extent to which these local changes are coupled to additional changes in the structure/dynamics of the repressor was investigated using hydrogen/deuterium exchange coupled to mass spectrometry. Measurements were performed on the apo-protein and on complexes of the protein bound to four different effectors that elicit a range of thermodynamic response

SUBMITTER: Laine O 

PROVIDER: S-EPMC2735192 | biostudies-literature | 2008 Aug

REPOSITORIES: biostudies-literature