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This study focuses on the differential allosteric regulation by the ubiquitous signaling molecule, cAMP, in the cAMP receptor protein from Escherichia coli (CRPEcoli) and from Mycobacterium tuberculosis (CRPMTB). By introducing structurally homologous mutations from allosteric hotspots previously identified in CRPEcoli into CRPMTB and examining their effects on protein solution structure, stability, and function, we aimed to determine the factors contributing to their differential allosteric regulation. Results from this study indicate that the structural similarity between two allosteric proteins from distantly related bacteria does not reliably predict their allosteric behavior nor identify allosteric hotspots involved in the response to molecular signals.

Identifying Allosteric Hotspots in Mycobacterium tuberculosis cAMP Receptor Protein through Structural Homology

This study focuses on the differential allosteric regulation by the ubiquitous signaling molecule, cAMP, in the cAMP receptor protein from Escherichia coli (CRPEcoli) and from Mycobacterium tuberculosis (CRPMTB). By introducing structurally homologous mutations from allosteric hotspots previously identified in CRPEcoli into CRPMTB and examining their effects on protein solution structure, stability, and function, we aimed to determine the factors contributing to their differential allosteric regulation. Results from this study indicate that the structural similarity between two allosteric proteins from distantly related bacteria does not reliably predict their allosteric behavior nor identify allosteric hotspots involved in the response to molecular signals. 

Read more: Identifying Allosteric Hotspots in Mycobacterium tuberculosis cAMP Receptor Protein through Structural Homology | Biochemistry

Credit: Rodrigo Maillard

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This study focuses on the differential allosteric regulation by the ubiquitous signaling molecule, cAMP, in the cAMP receptor protein from Escherichia coli (CRPEcoli) and from Mycobacterium tuberculosis (CRPMTB). By introducing structurally homologous mutations from allosteric hotspots previously identified in CRPEcoli into CRPMTB and examining their effects on protein solution structure, stability, and function, we aimed to determine the factors contributing to their differential allosteric regulation. Results from this study indicate that the structural similarity between two allosteric proteins from distantly related bacteria does not reliably predict their allosteric behavior nor identify allosteric hotspots involved in the response to molecular signals.

Georgetown Researchers Uncover Key Differences in Bacterial Protein Regulation

February 11th, 2025

A new study led by Dr. Rodrigo Maillard at Georgetown University, “Identifying Allosteric Hotspots in Mycobacterium tuberculosis cAMP Receptor Protein through Structural Homology,” published in Biochemistry sheds light on how bacteria regulate their genes, challenging long-held assumptions about protein behavior. Published in Biochemistry, the research compares how two bacterial species—Escherichia coli and Mycobacterium tuberculosis—use a signaling molecule called cyclic AMP (cAMP) to control important cellular functions.…

Advancing Biomimetic Materials at Georgetown University

January 29th, 2025

Researchers within the Institute for Soft Matter Synthesis and Metrology (ISMSM) at Georgetown University, in collaboration with TU Eindhoven, have developed groundbreaking synthetic gel materials that mimic the dynamic properties of biological extracellular matrices. …

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