Sandbox Reserved 1069: Difference between revisions

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===Interlocking Salt Bridge===

The <scene name='75/756372/Saltbridgeclose/1'>salt bridge</scene> formation between Lys77 and Asp207 of each domain of YiiP form an interlocking interaction that acts as the pivot point of the conformational change that drives the function of YiiP. The salt bridge is disrupted when Zinc is bound, due to movement of the antiparallel helices. This disrupts the ion-ion attractions that established the salt bridge- causing a conformational shift in YiiP. This salt bridge also aids in holding the two monomers together. [[Image:Saltbridge.png|200px|left|thumb|Lys77 and Asp207 Salt Bridges]]<scene name='75/756372/Hydrophobic1/1'>Hydrophobic</scene> residues ~~beneath~~ the salt bridge further stabilize the two domains in the v-shaped void where the domains connect. This prevents degradation of the protein's interlock via interactions with the environment.

The <scene name='75/756372/Saltbridgeclose/1'>salt bridge</scene> formation between Lys77 and Asp207 of each domain of YiiP form an interlocking interaction that acts as the pivot point of the conformational change that drives the function of YiiP. The salt bridge is disrupted when Zinc is bound, due to movement of the antiparallel helices. This disrupts the ion-ion attractions that established the salt bridge- causing a conformational shift in YiiP. This salt bridge also aids in holding the two monomers together. [[Image:Saltbridge.png|200px|left|thumb|Lys77 and Asp207 Salt Bridges]]<scene name='75/756372/Hydrophobic1/1'>Hydrophobic</scene> residues around the salt bridge further stabilize the two domains in the v-shaped void where the domains connect. This prevents degradation of the protein's interlock via interactions with the environment.

=== Zinc Binding Sites ===

Sandbox Reserved 1069: Difference between revisions

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@@ Line 12: / Line 12: @@
 ===Interlocking Salt Bridge===
-The <scene name='75/756372/Saltbridgeclose/1'>salt bridge</scene> formation between Lys77 and Asp207 of each domain of YiiP form an interlocking interaction that acts as the pivot point of the conformational change that drives the function of YiiP. The salt bridge is disrupted when Zinc is bound, due to movement of the antiparallel helices. This disrupts the ion-ion attractions that established the salt bridge- causing a conformational shift in YiiP. This salt bridge also aids in holding the two monomers together. [[Image:Saltbridge.png|200px|left|thumb|Lys77 and Asp207 Salt Bridges]]<scene name='75/756372/Hydrophobic1/1'>Hydrophobic</scene> residues beneath the salt bridge further stabilize the two domains in the v-shaped void where the domains connect. This prevents degradation of the protein's interlock via interactions with the environment.
+The <scene name='75/756372/Saltbridgeclose/1'>salt bridge</scene> formation between Lys77 and Asp207 of each domain of YiiP form an interlocking interaction that acts as the pivot point of the conformational change that drives the function of YiiP. The salt bridge is disrupted when Zinc is bound, due to movement of the antiparallel helices. This disrupts the ion-ion attractions that established the salt bridge- causing a conformational shift in YiiP. This salt bridge also aids in holding the two monomers together. [[Image:Saltbridge.png|200px|left|thumb|Lys77 and Asp207 Salt Bridges]]<scene name='75/756372/Hydrophobic1/1'>Hydrophobic</scene> residues around the salt bridge further stabilize the two domains in the v-shaped void where the domains connect. This prevents degradation of the protein's interlock via interactions with the environment.
 === Zinc Binding Sites ===