1t28
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(New page: 200px<br /><applet load="1t28" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t28" /> '''High resolution structure of a picornaviral ...)
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Revision as of 23:23, 24 November 2007
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High resolution structure of a picornaviral internal cis-acting replication element
Overview
Picornaviruses constitute a medically important family of RNA viruses in, which genome replication critically depends on a small RNA element, the, cis-acting replication element (cre), that templates 3D(pol), polymerase-catalyzed uridylylation of the protein primer for RNA, synthesis, VPg. We report the solution structure of the 33-nt cre of human, rhinovirus 14 under solution conditions optimal for uridylylation in, vitro. The cre adopts a stem-loop conformation with an extended duplex, stem supporting a novel 14-nt loop that derives stability from, base-stacking interactions. Base-pair interactions are absent within the, loop, and base substitutions within the loop that favor such interactions, are detrimental to viral RNA replication. Conserved adenosines in the 5', loop sequence that participate in a slide-back mechanism of VPg-pUpU, synthesis are oriented to the inside of the loop but are available for, base templating during uridylation. The structure explains why, substitutions of the 3' loop nucleotides have little impact on, conformation of the critical 5' loop bases and accounts for wide variation, in the sequences of cres from different enteroviruses and rhinoviruses.
About this Structure
1T28 is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
High-resolution structure of a picornaviral internal cis-acting RNA replication element (cre)., Thiviyanathan V, Yang Y, Kaluarachchi K, Rijnbrand R, Gorenstein DG, Lemon SM, Proc Natl Acad Sci U S A. 2004 Aug 24;101(34):12688-93. Epub 2004 Aug 16. PMID:15314212
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