1t28
From Proteopedia
(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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'''High resolution structure of a picornaviral internal cis-acting replication element'''<br /> | '''High resolution structure of a picornaviral internal cis-acting replication element'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Picornaviruses constitute a medically important family of RNA viruses in | + | 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== | ==About this Structure== | ||
| - | 1T28 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1T28 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T28 OCA]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15314212 15314212] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15314212 15314212] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Gorenstein, D | + | [[Category: Gorenstein, D G.]] |
[[Category: Kaluarachchi, K.]] | [[Category: Kaluarachchi, K.]] | ||
| - | [[Category: Lemon, S | + | [[Category: Lemon, S M.]] |
[[Category: Reynbrand, R.]] | [[Category: Reynbrand, R.]] | ||
[[Category: Thiviyanathan, V.]] | [[Category: Thiviyanathan, V.]] | ||
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[[Category: stem loop]] | [[Category: stem loop]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:09:06 2008'' |
Revision as of 13:09, 21 February 2008
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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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