Sandbox Reserved 1069: Difference between revisions
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The salt bridge formation between Lys77 and Asp207 of each domain of YiiP form an interlocking salt bridge 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 protomers together. [[Image:Saltbridge.png|200px|left|thumb|Lys77 and Asp207 Salt Bridges]] | The salt bridge formation between Lys77 and Asp207 of each domain of YiiP form an interlocking salt bridge 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 protomers together. [[Image:Saltbridge.png|200px|left|thumb|Lys77 and Asp207 Salt Bridges]] | ||
===Hydrophobic Residues==== | ====Hydrophobic Residues==== | ||
<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. | <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. | ||
