A Molecular Docking Study between Heavy Metals and Hydrophilic Hsp70 Protein to Explore Binding Pockets

Abstract

Abstract Microorganisms are abundant resident of whole biosphere and exert influential activity on various numerous biological phenomena. Sources of heavy metal contaminants include refineries, effluent outfalls from factories, waste treatment facilities and different anthropogenic products. Heavy metal pollution is now getting a prime concern for whole world including India also. For example, increased levels of lead, cadmiumfound in river ecosystem of West Bengal. The non-essential minerals cadmium (Cd), lead (Pb)linkedwith damageof vital organs. Remediation of pollutant is required to clean up society. Bioremediation includes use of biological agents such as bacteria are an essential component in the removal process of the contaminants. It is demonstrated that thermophilic bacteria secrete some special protein like heat shock protein to inhale such stress condition. Microbial Hsp70 (DnaK) proteins function to degrade noxious chemicals including heavy metals. Archaeal and bacterial Hsp70 proteins were retrieved and named as BHSP70 to explore and analyze. Three-dimensional structure and quality of protein was predicted and validated. BHSP70-114 of Sulfobacillus acidophilus was selected for metal docking study to visualize their multi-metal resistance capabilities. Best docked model of Hsp70 protein with heavy metals was evaluated with PyMolto inspect the intramolecular interaction. In this in silicostudy, few recognized key amino acid residues like Asp, Asn, Glu, Gln, His, Ser, Cys, Ala were identified, involve in heavy metal (Cd, Pb) binding. Recent approach also provides an important basis to inspect protein engineering for optimum use of bacterial Hsp70 protein to reduce or remove heavy metals from biosphere.