Abstract
The phage shock protein (Psp) is a part of the Psp operon, which assists in safeguarding the survival of bacterium in stress and shields the cell against proton motif force challenge. It is strongly induced by bacterium allied phages, improperly localized mutant porins and various other stresses. Master effector of the operon, PspA has been modeled and simulated, illustrating how it undergoes significant conformational transition at the far end in Mycobacterium tuberculosis. Association of this key protein of the operon influences action of Psp system on the whole. We are further working on the impact of phosphorylation perturbation and changes in the structure of PspA during complex formation with other moieties of interest.
Copyright
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC 4.0 International license.
Posted May 05, 2016.
Understanding properties of the master effector of phage shock operon in Mycobacterium tuberculosis via bioinformatics approach
