Sandbox Reserved 1559: Difference between revisions

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[[Image:6ojtsecondarystructure.png|600 px]]

The tertiary structure creates a<scene name='82/823083/Aminobindingpocket/1'> binding pocket of amino acids</scene> that are important to the active site. His282 provides pi-stacking, Phe305 provides Hydrophobic contacts, and Tyr101 provides Hydrogen bonding. The tertiary structure also allows the NSL ligand to interact using its 4-hydroxy with the catalytic triad. LsdA can only cleave 4-hydroxystilbenes. The photo below shows the NSL ligand interacting in the binding pocket~~, and it also shows the orange heme interacting with the amino group on the ligand~~.

The tertiary structure creates a<scene name='82/823083/Aminobindingpocket/1'> binding pocket of amino acids</scene> that are important to the active site. His282 provides pi-stacking, Phe305 provides Hydrophobic contacts, and Tyr101 provides Hydrogen bonding. The tertiary structure also allows the NSL ligand to interact using its 4-hydroxy with the catalytic triad. LsdA can only cleave 4-hydroxystilbenes. The photo below shows the NSL ligand interacting in the binding pocket.

[[Image:NSL_ligand.png|600 px]]

The tertiary structure also creates a metal binding site of Histidines to keep the iron molecule in place. There have been two mechanisms proposed for Lsd's. In one mechanism, the hydroxystillbenoid is activated via the enzyme-catalyzed deprotonation of the 4-hydroxy group, which then allows electron delocalization toward an Fe3+. In the other mechanism, π electron density from the double bond is redistributed to the iron-oxy complex to form an Fe2+ cation intermediate. Deprotonation of the hydroxyl is demanding for both mechanisms and is assisted by Lys134 and Tyr101.

[[Image:Example.jpg]]

== Energy Transformation ==

Sandbox Reserved 1559: Difference between revisions

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@@ Line 19: / Line 19: @@
 [[Image:6ojtsecondarystructure.png|600 px]]
-The tertiary structure creates a<scene name='82/823083/Aminobindingpocket/1'> binding pocket of amino acids</scene> that are important to the active site. His282 provides pi-stacking, Phe305 provides Hydrophobic contacts, and Tyr101 provides Hydrogen bonding. The tertiary structure also allows the NSL ligand to interact using its 4-hydroxy with the catalytic triad. LsdA can only cleave 4-hydroxystilbenes. The photo below shows the NSL ligand interacting in the binding pocket, and it also shows the orange heme interacting with the amino group on the ligand.
+The tertiary structure creates a<scene name='82/823083/Aminobindingpocket/1'> binding pocket of amino acids</scene> that are important to the active site. His282 provides pi-stacking, Phe305 provides Hydrophobic contacts, and Tyr101 provides Hydrogen bonding. The tertiary structure also allows the NSL ligand to interact using its 4-hydroxy with the catalytic triad. LsdA can only cleave 4-hydroxystilbenes. The photo below shows the NSL ligand interacting in the binding pocket.
 [[Image:NSL_ligand.png|600 px]]
+The tertiary structure also creates a metal binding site of Histidines to keep the iron molecule in place. There have been two mechanisms proposed for Lsd's. In one mechanism, the hydroxystillbenoid is activated via the enzyme-catalyzed deprotonation of the 4-hydroxy group, which then allows electron delocalization toward an Fe3+. In the other mechanism, π electron density from the double bond is redistributed to the iron-oxy complex to form an Fe2+ cation intermediate. Deprotonation of the hydroxyl is demanding for both mechanisms and is assisted by Lys134 and Tyr101.
+[[Image:Example.jpg]]
 == Energy Transformation ==