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Some ATPases work in reverse, using the energy from the hydrolysis of ATP to create a proton gradient. There are different types of ATPases, which can differ in function (ATP synthesis and/or hydrolysis), structure (F-, V- and A-ATPases contain rotary motors) and in the type of ions they transport. [3] [4] The types with this domain include:
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Most useful ATP analogs cannot be hydrolyzed as ATP would be; instead, they trap the enzyme in a structure closely related to the ATP-bound state. Adenosine 5′-(γ-thiotriphosphate) is an extremely common ATP analog in which one of the gamma-phosphate oxygens is replaced by a sulfur atom; this anion is hydrolyzed at a dramatically slower rate ...
The structure of the intact ATP synthase is currently known at low-resolution from electron cryo-microscopy (cryo-EM) studies of the complex. The cryo-EM model of ATP synthase suggests that the peripheral stalk is a flexible structure that wraps around the complex as it joins F 1 to F O.
ADP and Pi (inorganic phosphate) bind spontaneously to the three β subunits of the F 1 domain, so that every time it goes through a 120° rotation ATP is released (rotational catalysis). The F o domains sits within the membrane, spanning the phospholipid bilayer, while the F 1 domain extends into the cytosol of the cell to facilitate the use ...
Molecular structure of adenosine triphosphate (ATP) An ATP-binding motif is a 250-residue sequence within an ATP-binding protein’s primary structure. The binding motif is associated with a protein’s structure and/or function. [1] ATP is a molecule of energy, and can be a coenzyme, involved in a number of biological reactions.
The chemical structure of adenosine triphosphate. Date: 16 August 2007: Source: Self-made in bkchem; edited in perl. Author: Mysid: Other versions: Derivative works of this file: ATP structure revised.png: SVG development
F-ATP synthases are identical in appearance and function except for the mitochondrial F 0 F 1-ATP synthase, which contains 7-9 additional subunits. [12] The electrochemical potential is what causes the c-ring to rotate in a clockwise direction for ATP synthesis. This causes the central stalk and the catalytic domain to change shape.