Sandbox Reserved 1684: Difference between revisions
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==Viral RNA Classification== | ==Viral RNA Classification== | ||
The poliovirus comes in three different serotypes: poliovirus 1 (PV1), poliovirus 2 (PV2), or poliovirus 3 (PV3). These viruses are non-enveloped, single-stranded positive-sense RNA. The poliovirus is a member of the picornavirus family which includes a significant number of pathogens for humans and livestock. This virus is very small and consists of an icosahedral protein coat. | The poliovirus comes in three different serotypes: poliovirus 1 (PV1), poliovirus 2 (PV2), or poliovirus 3 (PV3). These viruses are non-enveloped, single-stranded positive-sense RNA. The poliovirus is a member of the picornavirus family which includes a significant number of pathogens for humans and livestock. This virus is very small and consists of an icosahedral protein coat. The 7500 nucleotide single-strand RNA genome of poliovirus contains one long open reading frame which is translated into a 247 kDa polyprotein. | ||
== RNA-Dependent RNA Polymerase Function == | == RNA-Dependent RNA Polymerase Function == | ||
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== Structural Features == | == Structural Features == | ||
The Poliovirus RNA-Dependent RNA polymerase is a 53kDa polymerase which together with other host proteins carries out viral RNA replication on the host cell cytoplasm. The poliovirus RdRp’s shape is common to that of other polymerases, with a palm subdomain which contains a core structure very similar to other polymerases, and different structures of the fingers and thumb from those of other polymerases. | The Poliovirus RNA-Dependent RNA polymerase is a 53kDa polymerase which together with other host proteins carries out viral RNA replication on the host cell cytoplasm. The poliovirus RdRp’s shape is common to that of other polymerases, with a palm subdomain which contains a core structure very similar to other polymerases, and different structures of the fingers and thumb from those of other polymerases. | ||
The palm subdomain contains five of the amino acid sequence <scene name='89/891374/Motifs/5'>motifs</scene> of RNA-dependent RNA polymerases, referred to as A, B, C, D, and E. The thumb subdomain is composed of mostly residues C-terminal of the palm subdomain and is largely alpha helical. The core structure comprises motifs A-D, and it consists of two alpha helices that pack beneath a four-stranded antiparallel beta sheet. The strands of the antiparallel beta sheet are composed of residues from motifs A, C, and part of D, while the alpha helices are composed of residues from motif B and the remainder of motif D. Motif E packs between the pal and thumb subdomains. Near the end of the beta strand of motif A just before the helix is a completely conserved aspartate residue that is expected to coordinate catalytically essential metal ions. | The palm subdomain contains five of the amino acid sequence <scene name='89/891374/Motifs/5'>motifs</scene> of RNA-dependent RNA polymerases, referred to as A, B, C, D, and E. The thumb subdomain is composed of mostly residues C-terminal of the palm subdomain and is largely alpha helical. The core structure comprises motifs A-D, and it consists of two alpha helices that pack beneath a four-stranded antiparallel beta sheet. The strands of the antiparallel beta sheet are composed of residues from motifs A, C, and part of D, while the alpha helices are composed of residues from motif B and the remainder of motif D. Motif E packs between the pal and thumb subdomains. Near the end of the beta strand of motif A just before the helix is a completely conserved aspartate residue that is expected to coordinate catalytically essential metal ions. | ||
