Sandbox Reserved 1059: Difference between revisions
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===Conserved Motifs=== | ===Conserved Motifs=== | ||
Members of the NrdH family are typically characterized by CVQC and WSGFRP sequence motifs. The residues between the two cysteines are known to affect redox potentials and pKa values. Also, by changing the target proteins, in turn, they regulate the function. The N-terminal cysteine acts as a nucleophile, whereas the C-terminal cysteine acts as a resolving cysteine. <ref>DOI 10.1021/bi400191z</ref> | Members of the NrdH family are typically characterized by CVQC and WSGFRP <scene name='69/694226/Conserved_motifs/1'>conserved sequence motifs.</scene> | ||
Within the CVQC motif, the amide oxygen of glutamine residue is firmly hydrogen bonded with the peptidyl nitrogen of Phe-44. The amide nitrogen of glutamine is then available for further hydrogen bonding. The carbonyl oxygen of Val-12 hydrogen bonds with peptidyl nitrogen of Ala-16. | |||
<ref>DOI 10.1021/bi400191z</ref> . The residues between the two cysteines are known to affect redox potentials and pKa values. Also, by changing the target proteins, in turn, they regulate the function. The N-terminal cysteine acts as a nucleophile, whereas the C-terminal cysteine acts as a resolving cysteine. <ref>DOI 10.1021/bi400191z</ref> | |||
The WSGFRP motif 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. This hydrogen bonding network lends to the stability of the redox active site.<ref>DOI 10.1021/bi400191z</ref> | The WSGFRP motif 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. This hydrogen bonding network lends to the stability of the redox active site.<ref>DOI 10.1021/bi400191z</ref> | ||
