Structural insights into the mechanism of the allosteric transitions of Mycobacterium tuberculosis cAMP receptor protein.

ABSTRACT: The cAMP receptor protein (CRP) from Mycobacterium tuberculosis is a cAMP-responsive global transcriptional regulator, responsible for the regulation of a multitude of diverse proteins. We have determined the crystal structures of the CRP.cAMP and CRP.N(6)-cAMP derivative-bound forms of the enzyme to 2.2- and 2.3 A-resolution, respectively, to investigate cAMP-mediated conformational and structural changes. The allosteric switch from the open, inactive conformation to the closed, active conformation begins with a number of changes in the ligand-binding cavity upon cAMP binding. These subtle structural changes and numerous non-bonding interactions between cAMP, the N-domain residues, and the C-domain helices demonstrate that the N-domain hairpin loop acts as a structural mediator of the all

SUBMITTER: Reddy MCM 

PROVIDER: S-EPMC2794773 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature