Quantum Transition in Zinc Atoms of Flavavirus Polymerase Triggers the Conformation of the Polymerase Motif F
Flavavirus RdRp contains two zinc atoms located in two specific zinc binding sites in the protein. Molecular dynamics experiments with flavavirus RdRp suggest that the conformation of the conservative motif F in the polymerase is highly sensitive to the bond lengths between the zinc atoms and their four coordinating atoms. In the experimental structures of flavavirus RdRp, motif F is presented in two different conformations. The polymerase acts as a catalyst only in one of the motif F conformations. We hypothesize that the second conformation is required for the formation of the viral replicative complex and that it is the quantum transition in the zinc atoms which slightly changes the bond lengths; thus assisting the switch between the two motif F conformations.