In silico study of cox protein from P2 type enteric bacteriophages based on sequence, structure and dynamics to...

Area of Science:

• Molecular Biology
• Structural Biology
• Bioinformatics

Background:

• Cox protein controls the lytic-lysogenic switch in P2 enteric phages.
• Its DNA-binding activity regulates promoter expression, crucial for phage lifecycle.
• Cox protein is a promising target for novel phage-based therapeutics against antibiotic-resistant bacteria.

Purpose of the Study:

• To elucidate the sequence, structural, and dynamic features of Cox protein's DNA binding.
• To build a comprehensive Cox protein database through extensive literature review.
• To provide a foundation for understanding Cox protein activation and designing phage therapeutics.

Main Methods:

• Sequence-based phylogenetic and conservation analyses.
• Homology modeling for structural prediction.
• Atomic-level docking and extensive Molecular Dynamics (MD) simulations (500 ns total).

Main Results:

• Integrated sequence, structure, and dynamics data for Cox protein.
• Detailed understanding of the sequence-to-structure-to-dynamics-to-function relationship.
• Identification of key features for Cox protein's DNA binding and activation.

Conclusions:

• The study provides crucial biochemical insights into Cox protein activation.
• Findings facilitate the rational design of advanced phage-based therapeutics.
• This research supports the development of new strategies against resistant pathogens.