title: Conformational changes in motif D of RdRPs as fidelity determinant.
abstract: RNA-dependent RNA polymerases (RdRPs) are the central players in both transcription and viral genome replication. Using NMR spectroscopy, Yang and colleagues (in this issue of Structure) show that the conformational changes in the structural motif D of poliovirus RdRP correlate with the nature of the bound nucleotide (correct versus incorrect), with a conserved lysine within this motif playing a key role.
authors.affiliation: Institut de Biologia Molecular de Barcelona (CSIC), Parc Científic de Barcelona, Baldiri i Reixac 10, E-08028 Barcelona, Spain. nvmcri@ibmb.csic.es
authors.forename: Nuria
authors.initials: N
authors.lastname: Verdaguer
authors.forename: Cristina
authors.initials: C
authors.lastname: Ferrer-Orta
mesh_terms: D009711:Nucleotides / Q000737:chemistry*; D017955:Poliovirus / Q000201:enzymology*; D012324:RNA-Dependent RNA Polymerase / Q000737:chemistry*
chemical_list: D009711:Nucleotides; D012324:RNA-Dependent RNA Polymerase