Sandbox Reserved 1051: Difference between revisions

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The mutant [http://proteopedia.org/wiki/index.php/4qdo Ag85C-Hg] (Figure 5) is generated with the addition of [http://en.wikipedia.org/wiki/4-Chloromercuribenzoic_acid p-chloromercuribenzoic acid] (Figure 6), the side chain of the complex is disordered due to a lack of hydrogen bonds between Glu228 and His260. Similar to what is observed in Ag85C-ebselen, the alteration in <scene name='69/694218/~~Ag85c-hg~~/1'>Ag85C-Hg</scene> relaxes the kinked helix α-9 found in the native structure of the enzyme, thus inhibiting the active site (Figure 7). The ultimate effect is a decrease to only 60% of the normal enzymatic function of Ag85C.<ref name="Favrot"/>

The mutant [http://proteopedia.org/wiki/index.php/4qdo Ag85C-Hg] (Figure 5) is generated with the addition of [http://en.wikipedia.org/wiki/4-Chloromercuribenzoic_acid p-chloromercuribenzoic acid] (Figure 6), the side chain of the complex is disordered due to a lack of hydrogen bonds between Glu228 and His260. Similar to what is observed in Ag85C-ebselen, the alteration in <scene name='69/694218/4qdo/1'>Ag85C-Hg</scene> relaxes the kinked helix α-9 found in the native structure of the enzyme, thus inhibiting the active site (Figure 7). The ultimate effect is a decrease to only 60% of the normal enzymatic function of Ag85C.<ref name="Favrot"/>

===Ag85C-E228Q===

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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.]]

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"/>

In <scene name='69/694218/Mutationh260q/1'>Ag85C-H260Q</scene> (Figure 10), a shift in helix α-9 <scene name='69/694218/Ag85c-hg/1'>prevents the hydrogen bond formation</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>

Sandbox Reserved 1051: Difference between revisions

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@@ Line 49: / Line 49: @@
-The mutant [http://proteopedia.org/wiki/index.php/4qdo Ag85C-Hg] (Figure 5) is generated with the addition of [http://en.wikipedia.org/wiki/4-Chloromercuribenzoic_acid p-chloromercuribenzoic acid] (Figure 6), the side chain of the complex is disordered due to a lack of hydrogen bonds between Glu228 and His260.  Similar to what is observed in Ag85C-ebselen, the alteration in <scene name='69/694218/Ag85c-hg/1'>Ag85C-Hg</scene> relaxes the kinked helix α-9 found in the native structure of the enzyme, thus inhibiting the active site (Figure 7).  The ultimate effect is a decrease to only 60% of the normal enzymatic function of Ag85C.<ref name="Favrot"/>
+The mutant [http://proteopedia.org/wiki/index.php/4qdo Ag85C-Hg] (Figure 5) is generated with the addition of [http://en.wikipedia.org/wiki/4-Chloromercuribenzoic_acid p-chloromercuribenzoic acid] (Figure 6), the side chain of the complex is disordered due to a lack of hydrogen bonds between Glu228 and His260.  Similar to what is observed in Ag85C-ebselen, the alteration in <scene name='69/694218/4qdo/1'>Ag85C-Hg</scene> relaxes the kinked helix α-9 found in the native structure of the enzyme, thus inhibiting the active site (Figure 7).  The ultimate effect is a decrease to only 60% of the normal enzymatic function of Ag85C.<ref name="Favrot"/>
 ===Ag85C-E228Q===
@@ Line 65: / Line 65: @@
 [[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 <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"/>
+In <scene name='69/694218/Mutationh260q/1'>Ag85C-H260Q</scene> (Figure 10), a shift in helix α-9 <scene name='69/694218/Ag85c-hg/1'>prevents the hydrogen bond formation</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>