Abstract:
Myosin is an ATPase motor protein present in all eukaryotes. It has a unique ability of coupling four-state ATP hydrolysis cycle with hand-over-hand walking movement and force generation on actin filament. Beneath these mechanical properties exists an intricate allosteric mechanism. Our study aims to elucidate unexplored allosteric conformational changes and to predict crucial residues responsible for this conformational change and validate them through mutation studies. By carrying out comprehensive structural analysis, we came up with a residue connection pathway that allows coupling between active site and actin binding region. Furthermore, validation of this pathway through in vivo mutational studies on Myo2p protein in fission yeast further supported the importance of the residue connection pathway.
