Long-range interaction networks in the function and fidelity of poliovirus RNA-dependent RNA polymerase studied by nuclear magnetic resonance

NMR studies with [methyl-[super 13C]]methionine-labeled protein are used for comparing the solution structure and dynamics of wild-type and a single site mutation (Gly64Ser) of the poliovirus RNA-dependent RNA polymerase (3[D.sup.pol]). The studies have shown that there is a long-distance network operating throughout 3[D.sup.pol] that has coordinated ligand binding, conformational changes and catalysis and the mutation of Gly64 has resulted in structural and dynamic changes to the network that might affect polymerase fidelity.