Abstract
Bacillus anthracis is a pathogenic, Gram-positive bacterium which chiefly affects the livestock of animals and humans through acute disease anthrax. All around the globe this bio-threat organism damages millions of lives in every year and also most of the drugs were not responding properly in inhibition against this diseased pathogen. In recent development, phage therapy is considered as alternative solution to treat this serious infectious disease. In this study, we elucidated the binding of γ phage lysin plyG enzymes toward the SrtA along with its activator peptide LPXTG. Through protein–protein docking and molecular dynamics simulation studies, we showed the distinguished structure complementarity of SrtA and plyG complex. Especially, MD simulation relates strong and stable interaction occurs between the protein complex structures. These results suggest that additional experimental studies on our approach will lead to availability of better inhibitor against the SrtA.
Acknowledgment
Chandrabose Selvaraj gratefully acknowledges CSIR for the Senior Research Fellowship (SRF). R. Bharathipriya Sincerely thank the facillities offered by the UGC Innovative program in Department of Bioinformatics, Alagappa University.
Declaration of interest: The author report no declaration of interest. The author alone is responsible for the content and writing of the paper.
This Research work was partially supported by a Council of Scientific & Industrial Research, India (CSIR sanction no: 37(1491)/11/EMR-II), and Dr. Sanjeev Kumar Singh acknowledging CSIR for financial support.