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Sandbox Reserved 1684
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The palm subdomain contains five of the amino acid sequence <scene name='89/891374/Motifs/2'>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/2'>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 fingers subdomain of the poliovirus RdRp is composed of two polypeptide segments, a larger segment that precedesmotif A and a smaller segment composed of residues between motifs A and B of the palm subdomain.This fingers subdomain is composed of two polypeptide segments, an N-terminal of the palm subdomain and the second between motifs A and B. The thumb subdomain is composed primarily ofthe C-terminal-most 80 amino acid residues. The thumb subdomain of this polymerase begins with a beta strand that interacts with the edge of the beta strands of motif E to from a short three-stranded antiparallel beta sheet. The remainder of the thumb is composed of a series of five alpha helices. The first three from a three-helix bundle, the fourth is positioned at the top of the thumb subdomain and the fifth is positioned along the front edge of the beta strand of the thumb subdomain. | + | The <scene name='89/891374/Fingers/4'>fingers subdomain</scene> of the poliovirus RdRp is composed of two polypeptide segments, a larger segment that precedesmotif A and a smaller segment composed of residues between motifs A and B of the palm subdomain.This fingers subdomain is composed of two polypeptide segments, an N-terminal of the palm subdomain and the second between motifs A and B. The thumb subdomain is composed primarily ofthe C-terminal-most 80 amino acid residues. The thumb subdomain of this polymerase begins with a beta strand that interacts with the edge of the beta strands of motif E to from a short three-stranded antiparallel beta sheet. The remainder of the thumb is composed of a series of five alpha helices. The first three from a three-helix bundle, the fourth is positioned at the top of the thumb subdomain and the fifth is positioned along the front edge of the beta strand of the thumb subdomain. |
Revision as of 19:51, 11 October 2021
| This Sandbox is Reserved from 09/01/2021 through 12/01/2021 for use in Che 462 taught by Ann Taylor at Wabash College, Crawfordsville, IN USA. This reservation includes Sandbox Reserved 1683 through Sandbox Reserved 1689. |
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Poliovirus RNA-Dependent RNA Polymerase
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