Sandbox Reserved 1058: Difference between revisions

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===Active Site Residues===

[[Image:Active Loop Shift.png|250 px|left|thumb|'''Figure 2. Active Site Loop Shift.''' Binding of the ligand to the enzyme results in a conformational shift that facilitates the breakdown of isocitrate. The active site loop unbound is shown in wheat and the active site loop bound is shown in green.]][[Image:Active_Site_Hydrogen_Bonding.png|250 px|right|thumb|'''Figure 3. Active site residues hydrogen bound to a cofactor and the products of the catalyzed isocitrate reaction.''' Glyoxylate is shown in blue, succinate is shown in green, and the Mg<sup>2+</sup> cofactor is shown in yellow.]]

[[Image:Active_Site_Hydrogen_Bonding.png|250 px|right|thumb|'''Figure 3. Active site residues hydrogen bound to a cofactor and the products of the catalyzed isocitrate reaction.''' Glyoxylate is shown in blue, succinate is shown in green, and the Mg<sup>2+</sup> cofactor is shown in yellow.]]

[[Image:Active Site Residues.png|250 px|left|thumb|'''Figure 4. Active Site Residues.''' All eight active site residues necessary for catalysis of isocitrate are shown in slate. However, the protein shown is a C191S mutant of isocitrate lyase.]]

[[Image:Active Loop Shift.png|250 px|left|thumb|'''Figure 2. Active Site Loop Shift.''' Binding of the ligand to the enzyme results in a conformational shift that facilitates the breakdown of isocitrate. The active site loop unbound is shown in wheat and the active site loop bound is shown in green.]]

Sandbox Reserved 1058: Difference between revisions

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@@ Line 12: / Line 12: @@
 ===Active Site Residues===
-[[Image:Active Loop Shift.png|250 px|left|thumb|'''Figure 2. Active Site Loop Shift.''' Binding of the ligand to the enzyme results in a conformational shift that facilitates the breakdown of isocitrate. The active site loop unbound is shown in wheat and the active site loop bound is shown in green.]][[Image:Active_Site_Hydrogen_Bonding.png|250 px|right|thumb|'''Figure 3. Active site residues hydrogen bound to a cofactor and the products of the catalyzed isocitrate reaction.''' Glyoxylate is shown in blue, succinate is shown in green, and the Mg<sup>2+</sup> cofactor is shown in yellow.]]
+[[Image:Active_Site_Hydrogen_Bonding.png|250 px|right|thumb|'''Figure 3. Active site residues hydrogen bound to a cofactor and the products of the catalyzed isocitrate reaction.''' Glyoxylate is shown in blue, succinate is shown in green, and the Mg<sup>2+</sup> cofactor is shown in yellow.]]
 [[Image:Active Site Residues.png|250 px|left|thumb|'''Figure 4. Active Site Residues.''' All eight active site residues necessary for catalysis of isocitrate are shown in slate. However, the protein shown is a C191S mutant of isocitrate lyase.]]
+[[Image:Active Loop Shift.png|250 px|left|thumb|'''Figure 2. Active Site Loop Shift.''' Binding of the ligand to the enzyme results in a conformational shift that facilitates the breakdown of isocitrate. The active site loop unbound is shown in wheat and the active site loop bound is shown in green.]]