Sandbox Reserved 1051: Difference between revisions
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[[Image:H260Q zoom.png|100 xp|left|thumb|'''Figure 11.''' [http://proteopedia.org/wiki/index.php/4qe3 Ag85C-H260Q] active site. A shift in helix α-9 prevents formation of any stabilizing hydrogen bonds between residues His260 and Glu228, thus decreasing its enzymatic activity.]] | [[Image:H260Q zoom.png|100 xp|left|thumb|'''Figure 11.''' [http://proteopedia.org/wiki/index.php/4qe3 Ag85C-H260Q] active site. A shift in helix α-9 prevents formation of any stabilizing hydrogen bonds between residues His260 and Glu228, thus decreasing its enzymatic activity.]] | ||
In <scene name='69/694218/Mutationh260q/1'>Ag85C-H260Q</scene> (Figure 10), a shift in helix α-9 prevents the formation of any stabilizing hydrogen bonds between residues His260 and Glu228, thus decreasing its enzymatic activity (Figure 11). The conversion of the glutamate, a key player in the catalytic triad, to the corresponding amide-containing side chain as well as a loss of a general base in the charge relay are both key causes for the loss of function.<ref name="Favrot"/> | In <scene name='69/694218/Mutationh260q/1'>Ag85C-H260Q</scene> (Figure 10), a shift in helix α-9 <scene name='69/694218/4qe3/2'>prevents the formation of any stabilizing hydrogen bonds</scene> between residues His260 and Glu228, thus decreasing its enzymatic activity (Figure 11). The conversion of the glutamate, a key player in the catalytic triad, to the corresponding amide-containing side chain as well as a loss of a general base in the charge relay are both key causes for the loss of function.<ref name="Favrot"/> | ||
</StructureSection> | </StructureSection> | ||