Heat Shock Proteins 70 (HSP70) are found in nearly all living organisms. As molecular chaperones, they help nascent proteins adopt their functional three-dimensional conformations, they inhibit the aggregation of newly synthesized polypeptides, and help to prevent denaturation of cellular proteins under stressful conditions. Under more extreme environments, HSP70 also directs the degradation of irreversibly denatured proteins. The action of HSP70 is typically dependent upon its association with other molecular chaperones, and its binding to damaged or unfolded client proteins is modulated by its N-terminal nucleotide-binding domain’s ATPase activity. The aim of this study was to determine the physicochemical properties of HSP70 from the marine cyanobacterium Synechococcus WH5701 and to develop a three-dimensional model. Multiple sequence alignments revealed amino acid stretches that are unique to cyanobacterial HSP70s. Biocomputational studies were performed in silico using widely available software and servers. An analysis of the protein’s substrate-binding domain and nucleotide-binding residues will be presented along with the results of docking studies of the ATP-and ADP-bound protein.

Homology modelling and docking studies of nucleotide-bound HSP70 from the marine cyanobacterium Synechococcus WH5701

254th National Meeting (2017)

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