Conformational Changes in Motif D of RdRPs as Fidelity Determinant

descriptionPublicationkeyboard_double_arrow_right Article 01 Sep 2012 English Publisher:Elsevier BVJournal:Structure, volume 20, pages 1,448-1,450 (issn: 0969-2126,

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Authors: Verdaguer, Nuria; Ferrer-Orta, Cristina;

doi: 10.1016/j.str.2012.08.014

pmid: 22958639

handle: 10261/87792

Conformational Changes in Motif D of RdRPs as Fidelity Determinant

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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.

Related Organizations

Molecular Biology Institute of Barcelona
Spain
Spanish National Research Council
Spain

Keywords

Poliovirus, Structural Biology, Nucleotides, RNA-Dependent RNA Polymerase, Molecular Biology

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