Sandbox Reserved 1684: Difference between revisions

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Motif D of poliovirus polymerase forms an α helix-turn-β strand structure. The α helix packs beneath the β sheet of the core structure.The β strand of motif D makes limited antiparallel β sheet interactions with the outside of motif A to complete the four-stranded antiparallel β sheet of the core structure. The turn region packs against the base of the fingers subdomain.
Motif D of poliovirus polymerase forms an α helix-turn-β strand structure. The α helix packs beneath the β sheet of the core structure.The β strand of motif D makes limited antiparallel β sheet interactions with the outside of motif A to complete the four-stranded antiparallel β sheet of the core structure. The turn region packs against the base of the fingers subdomain.


 
Motif E is positioned between the palm and thumb subdomains and is not integral to the conserved core structure. Motif E forms a short β-turn-β structure that interacts extensively with the face of the β sheet of the core structure. These  interactions are distinctly hydrophobic and account for the conservation of several  hydrophobic residues in motifs A, C, and D of RNA-dependent polymerases.