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Journal of
eISSN: 2473-0831

Analytical & Pharmaceutical Research

Research Article Volume 3 Issue 7

Structural and Functional Analysis of Serine/Threonine Protein Kinase of Staphylococcus Aureus Exhibiting Variations with Other Bacterial PknB

Dudipeta Vasu, Pasupuleti Santhosh Kumar, Yellapu Nanda Kumar, Veeraraghavulu Praveen Chakravarthi, Potukuchi Venkata Gurunadha Krishna Sarma

Received: December 02, 2016 | Published: December 22, 2016

Citation: Vasu D, Kumar PS, Kumar YN, Chakravarthi VP, Sarma PVGK (2016) Structural and Functional Analysis of Serine/Threonine Protein Kinase of Staphylococcus aureus Exhibiting Variations with Other Bacterial PknB. J Anal Pharm Res 3(7): 00081. DOI: 10.15406/japlr.2016.03.00081

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Abstract

Staphylococcus aureusexpresses Serine-Threonine protein kinase (STPK) encoded by PknB gene in the extracellular filtrate and this enzyme is implicated in the expression of virulent factors, toxins and regulation of various metabolic pathways thereby creating anaerobic conditions which favours biofilm formation. Earlier we have cloned, sequenced (JN695616), expressed and characterized PknB gene of Staphylococcus aureus. The enzyme kinetics was established using synthetic peptide NLCNIPCSALLSSDITASVNCAK (stpks). The 3D structure of stpks was built using the amino acid sequence of stpks in Modeller 9v8. Further, stpks structure docked very close to the ATP binding site of STPK structure (PDB ID: 4EQM) with energy complex of -487.83Kcal/mol explaining the rapid transfer of γ-phosphate of ATP to its substrate therefore, proteins possessing STPK site would be highly vulnerable for phosphorylation by S. aureusPknB. Structural superimposition studies showed conspicuous variations were observed in STPK structure among bacteria as evidenced from the RMSD values which correlated with differences in the enzyme kinetics docking energy levels with substrate stpks. These differences indicate rate of phosphorylation among bacteria is variable which means factors contributing to pathogenesis are markedly different among bacteria.

Keywords: STPK, PknB, RMSD, ATP, Modeller9V.8, Phosphorylation, Superimposition, Conspicuous, Pathogenesis, STPK: Serine-Threonine Protein Kinase, RMSD: Root Mean Square Deviation, PIA: Polysaccharide Intracellular Adhesion, BHI: Brain Heart Infusion

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©2016 Vasu, et al. This is an open access article distributed under the terms of the, which permits unrestricted use, distribution, and build upon your work non-commercially.