Sandbox Reserved 1059: Difference between revisions

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The <scene name='69/694226/Cvqc_motif/3'>CVQC motif</scene>, is an active site and it is located at the N terminus of the first alpha helix<ref name="Laer" />. It is one of the best characterized redox motifs within the thioredoxin-like proteins. The N-terminal cysteine acts as a nucleophile and the C-terminal cysteine acts as the resolving cysteine. Valine is known to be exposed to the solvent. The hydrogen bonding network is important for stability to the redox active site <ref name="Phulera" />.

The <scene name='69/694226/Wsgfrp_conserved_motif/2'>WSGFRP ~~motif~~</scene> is stabilized by glutamine of the CVQC motif and phenylalanine is exposed to the solvent. Phe-64 and Val-12 with Ala-16 and Ala-20 create a distinct hydrophobic patch that is exposed to the solvent. This patch is of functional significance that could potentially interact with the C-terminus of RNR<ref name="Phulera" />.

The <scene name='69/694226/Wsgfrp_conserved_motif/3'>WSGFRP</scene> is stabilized by glutamine of the CVQC motif and phenylalanine is exposed to the solvent. Phe-64 and Val-12 with Ala-16 and Ala-20 create a distinct hydrophobic patch that is exposed to the solvent. This patch is of functional significance that could potentially interact with the C-terminus of RNR<ref name="Phulera" />.

In all members of the NrdH family, Arg-68 is a highly conserved residue. This residue hydrogen bonds with the main carbonyl oxygen of His-60, which is located before the WSGFRP motif. This suggests that the interaction between Arg-68 and His-60 may be of structural significance. In an alternate conformation of Arg-68, the guanidinyl group of Arg-68 forms a salt bridge with Asp-59. The hydrogen bonds and salt bridge work together to stabilize the WSGFRP motif <ref name="Phulera" />.

Sandbox Reserved 1059: Difference between revisions

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 The <scene name='69/694226/Cvqc_motif/3'>CVQC motif</scene>, is an active site and it is located at the N terminus of the first alpha helix<ref name="Laer" />. It is one of the best characterized redox motifs within the thioredoxin-like proteins. The N-terminal cysteine acts as a nucleophile and the C-terminal cysteine acts as the resolving cysteine. Valine is known to be exposed to the solvent. The hydrogen bonding network is important for stability to the redox active site <ref name="Phulera" />.
-The <scene name='69/694226/Wsgfrp_conserved_motif/2'>WSGFRP motif</scene> is stabilized by glutamine of the CVQC motif and phenylalanine is exposed to the solvent. Phe-64 and Val-12 with Ala-16 and Ala-20 create a distinct hydrophobic patch that is exposed to the solvent. This patch is of functional significance that could potentially interact with the C-terminus of RNR<ref name="Phulera" />.
+The <scene name='69/694226/Wsgfrp_conserved_motif/3'>WSGFRP</scene> is stabilized by glutamine of the CVQC motif and phenylalanine is exposed to the solvent. Phe-64 and Val-12 with Ala-16 and Ala-20 create a distinct hydrophobic patch that is exposed to the solvent. This patch is of functional significance that could potentially interact with the C-terminus of RNR<ref name="Phulera" />.
 In all members of the NrdH family, Arg-68 is a highly conserved residue. This residue hydrogen bonds with the main carbonyl oxygen of His-60, which is located before the WSGFRP motif. This suggests that the interaction between Arg-68 and His-60 may be of structural significance. In an alternate conformation of Arg-68, the guanidinyl group of Arg-68 forms a salt bridge with Asp-59.  The hydrogen bonds and salt bridge work together to stabilize the WSGFRP motif <ref name="Phulera" />.