B04 Dames: Regulation mechanisms and dynamic properties of mycobacterial protein kinase G
The eukaryotic-like ser/thr protein kinase G (PknG) allows survival of pathogenic mycobacteria such as M. tuberculosis in mammalian host cells by blocking their lysosomal degradation. The goal of the proposed structural and dynamic studies is to understand the role of phosphorylation in the natively unfolded N-terminus, of a specific threonine in the P+1 loop, and of the redox-sensitive rubredoxin motif for the regulation of kinase function. In addition, the importance of dynamic features for inhibitor binding is analysed. The expected data will provide general insights in kinase regulation by specific conformational switches and is of great interest for the design of new tuberculosis drugs for strains resistant to current therapies.