ArticleVirologica Sinica2017
Crystal structure of the coxsackievirus A16 RNA-dependent RNA polymerase elongation complex reveals novel features in motif A dynamics.
Article in Virologica Sinica, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Unusual substructure conformations observed in crystal structures of a dicistrovirus RNA-dependent RNA polymerase suggest contribution of the N-terminal extension in proper folding.Virologica Sinica · 2023Article
- Therapeutic targeting of measles virus polymerase with ERDRP-0519 suppresses all RNA synthesis activity.PLoS pathogens · 2021Article
- Structure of a paramyxovirus polymerase complex reveals a unique methyltransferase-CTD conformation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- A nucleobase-binding pocket in a viral RNA-dependent RNA polymerase contributes to elongation complex stability.Nucleic acids research · 2020Article
- A Structure-Function Diversity Survey of the RNA-Dependent RNA Polymerases From the Positive-Strand RNA Viruses.Frontiers in microbiology · 2019Review
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Authors and funding
3 authors.
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Abstract
The RNA-dependent RNA polymerases (RdRPs) encoded by RNA viruses represent a unique class of nucleic acid polymerases. Unlike other classes of single-subunit polymerases, viral RdRPs have evolved a unique conformational change in their palm domain to close the active site during catalysis. The hallmark of this conformational change is the backbone shift of the polymerase motif A from an "open" state to a "closed" state, allowing two universally conserved aspartic acid residues to orient toward each other for divalent metal binding and catalysis. The "closed" motif A conformation was only observed upon the binding of correct NTP in RdRP catalytic complexes or under rare conditions such as induced by a bound lutetium ion or a bound glutamate molecule. By solving the crystal structure of the catalytic elongation complex of the coxsackievirus RdRP, we in this work observed for the first time the "closed" motif A conformation in the absence of an NTP substrate or other conformational-change-inducing factors. This observation emphasizes the intrinsic dynamic features of viral RdRP motif A, and solidifies the structural basis for how this important structural element participates in catalytic events of the RdRPs.
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