A-ATP Synthase: Difference between revisions

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==~~F1F0~~ ATP Synthase==

==<scene name='A-ATP_Synthase/Rotary_stalk/1'>F1 ATP Synthase Rotary Mechanism</scene>==

The central stalk in ATP synthase, made of gamma, delta and epsilon subunits in the mitochondrial enzyme, is the key rotary element in the enzyme's catalytic mechanism. The ~~gamma~~ subunit penetrates the catalytic (alpha beta)(3) domain and protrudes beneath it, interacting with a ring of c subunits in the membrane that drives rotation of the stalk during ATP synthesis. The delta and epsilon subunits interact with a Rossmann fold in the gamma subunit, forming a foot. In ATP synthase, this foot interacts with the c-ring and couples the transmembrane proton motive force to catalysis in the (alpha beta)(3) domain.

The central stalk in ATP synthase, made of gamma, delta and epsilon subunits in the mitochondrial enzyme, is the key rotary element in the enzyme's catalytic mechanism. The <scene name='A-ATP_Synthase/Rotary_stalk/2'>Gamma subunit</scene> penetrates the catalytic (alpha beta)(3) domain and protrudes beneath it, interacting with a ring of c subunits in the membrane that drives rotation of the stalk during ATP synthesis. The delta and epsilon subunits interact with a Rossmann fold in the gamma subunit, forming a foot. In ATP synthase, this foot interacts with the c-ring and couples the transmembrane proton motive force to catalysis in the (<scene name='A-ATP_Synthase/Rotary_stalk/4'>alpha</scene> <scene name='A-ATP_Synthase/Rotary_stalk/3'>beta</scene>)(3) domain.

When operating as a generator, it uses the power of rotational motion to build ATP, or when operating as a motor, it breaks down ATP to spin the axle the opposite direction. The synthesis of ATP requires several steps, including the binding of ADP and phosphate, the formation of the new phosphate-phosphate bond, and release of ATP. As the axle turns, it '''forces the motor into three different conformations that assist these difficult steps.'''

A-ATP Synthase: Difference between revisions

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@@ Line 6: / Line 6: @@
 <StructureSection load=1e79 size='500' side='right' caption='F1-ATP synthase motor domain', ([[1e79]])' scene=''>
-==F1F0 ATP Synthase==
+==<scene name='A-ATP_Synthase/Rotary_stalk/1'>F1 ATP Synthase Rotary Mechanism</scene>==
-The central stalk in ATP synthase, made of gamma, delta and epsilon subunits in the mitochondrial enzyme, is the key rotary element in the enzyme's catalytic mechanism. The gamma subunit penetrates the catalytic (alpha beta)(3) domain and protrudes beneath it, interacting with a ring of c subunits in the membrane that drives rotation of the stalk during ATP synthesis. The delta and epsilon subunits interact with a Rossmann fold in the gamma subunit, forming a foot. In ATP synthase, this foot interacts with the c-ring and couples the transmembrane proton motive force to catalysis in the (alpha beta)(3) domain.
+The central stalk in ATP synthase, made of gamma, delta and epsilon subunits in the mitochondrial enzyme, is the key rotary element in the enzyme's catalytic mechanism. The <scene name='A-ATP_Synthase/Rotary_stalk/2'>Gamma subunit</scene> penetrates the catalytic (alpha beta)(3) domain and protrudes beneath it, interacting with a ring of c subunits in the membrane that drives rotation of the stalk during ATP synthesis. The delta and epsilon subunits interact with a Rossmann fold in the gamma subunit, forming a foot. In ATP synthase, this foot interacts with the c-ring and couples the transmembrane proton motive force to catalysis in the (<scene name='A-ATP_Synthase/Rotary_stalk/4'>alpha</scene> <scene name='A-ATP_Synthase/Rotary_stalk/3'>beta</scene>)(3) domain.
 When operating as a generator, it uses the power of rotational motion to build ATP, or when operating as a motor, it breaks down ATP to spin the axle the opposite direction. The synthesis of ATP requires several steps, including the binding of ADP and phosphate, the formation of the new phosphate-phosphate bond, and release of ATP. As the axle turns, it '''forces the motor into three different conformations that assist these difficult steps.'''