Identifying Allosteric Hotspots in <i>Mycobacterium tuberculosis</i> cAMP Receptor Protein through Structural Homology.

ABSTRACT: Understanding the mechanisms of allosteric regulation in response to second messengers is crucial for advancing basic and applied research. This study focuses on the differential allosteric regulation by the ubiquitous signaling molecule, cAMP, in the cAMP receptor protein from Escherichia coli (CRP_Ecoli) and from Mycobacterium tuberculosis (CRP_MTB). By introducing structurally homologous mutations from allosteric hotspots previously identified in CRP_Ecoli into CRP_MTB and examining their effects on protein solution structure, stability and function, we aimed to determine the factors contributing to their differential allosteric regulation. Our results demonstrate that the mutations did not significantly alter the overall fold, assem

SUBMITTER: Dokas SP 

PROVIDER: S-EPMC11840924 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature