Abstract 

Enzyme histidine kinase (HK) is essential to a bacterial two-component system. Due to its exclusive presence in microorganisms, it is considered a critical antimicrobial target. The primary role of HK is to take part in transducing signals in an NTP-dependent manner. As a phosphoryl donor HK family popularly uses Adenosine Triphosphate (ATP). Enzyme BA2291 from Bacillus anthracis is a rare exception that uses Guanosine Triphosphate (GTP). BA2291 is a part of the sporulation mechanism of B. anthracis. Sporulation regulates the transformation between the vegetative and spore-forming phases. Therefore, BA2291 plays an essential role in the survival of B. anthracis, making the protein a unique and exciting target for a novel antibacterial hunt. Utilizing the interdisciplinary in silico methods of Predictive Modeling, Docking, and Molecular Dynamics (MD), the present communication unravels the biochemical evidence behind its preference for GTP over ATP. Anthrax is a well-known life-threatening disease. However, this disease has yet to be wholly eradicated anthrax due to the deficiency of our understanding. The present study would be instrumental in unraveling the molecular basis for HK functioning and developing a platform for designing anti-anthrax therapeutics.

 

Keywords

 

BA2291, Bacillus anthracis, anthrax, molecular dynamics simulation, GTP, histidine kinase.

 

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