Alice Clark/ATPsynthase

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(New page: />{{Template:Protected page banner}} == '''ATP Synthase''' == <StructureSection load='5lqz' size='350' side='right' caption='Bovine (Cow) ATP Synthase (PDB entry 5lqz)' scene=''> s...)
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== '''ATP Synthase''' ==
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<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'>
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ATP synthase is shown here to the right ==>
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== '''ATP Synthase''' ==
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It is depicted in 3D with each protein shown in a different colour.
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<StructureSection load='5lqz' size='350' side='right' caption='Bovine (Cow) ATP Synthase (PDB entry [[5lqz]])' scene=''>
 
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stalk of the structure
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Tools for exploring ATP synthase in 3D
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membrane in bedded helices
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- left mouse button to rotate the protein model.
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adenosine diphosphate ADP
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- middle mouse button or scroll wheel to zoom (option-click on a Mac)
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adenosine triphosphate ATP
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- right mouse button for more options and information (control-click on a Mac).
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axle
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- green text - click to load a new 3D scene
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stator
 
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'''Have a go yourself now ==>'''
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To the right is a structure of ATP synthase shown using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].
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'''Exploring the ATP synthase molecule'''
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ATP synthase is a cellular molecular motor found in the mitochondrial membrane of humans, and also in other organisms. It has a role in the generation of ATP, the cells energy currency. This large molecule is built up of a number of different groups of proteins: the F0, the F1, and the stator - each group has an important role to play.
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Exploring in 3D
 
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- left mouse button to rotate the protein model.
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'''The F1 and Axle'''
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- middle mouse button or scroll wheel to zoom (option-click on a Mac)
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The <scene name='78/781973/Alpha-beta/1'>F1 motor head</scene> contains an α (alpha) chain (shown in light blue) and a β (beta) chain (shown in dark blue). The <scene name='78/781973/Axel/1'>axle</scene>, rotates (like the axle on a car), and is composed mainly of the <scene name='78/781973/Gamma/1'> γ (gamma) </scene> protein chain. The axle rotates with three 120° steps, putting the β chains into three different conformations, allowing the ADP and phosphate to bind, the high energy bond to form and the release of ATP.
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- right mouse button for more options and information (control-click on a Mac).
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'''Q1: Describe how the protein chains are arranged to comprise the F1 region?'''
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Have a go yourself now ==>
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----
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'''Q2: What is the role of the axle, explain how it acts on the β subunits?'''
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Click '>here</scene> for a view where the different components are coloured differently? See how many you can identify
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'''ADP and ATP are bound in the nucleotide binding sites'''
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The F1 shown here has both adenosine diphosphate (ADP) and adenosine triphosphate (ATP) bound in the <scene name='78/781973/Atpandadp/1'>nucleotide binding sites</scene>. See if you can zoom in on the ATP identify the phosphate atoms (orange), sugar moiety and the base moiety. ==>
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The three nucleotide binding sites, primarily located in the β subunits, carry out active ATP synthesis. The sites primarily located in the three α subunits are non-catalytic and exchange bound nucleotide very slowly. They are thought to be a carry over from evolution, and now play a more regulatory role.
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'''Q1: Where is the F1 region?'''
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'''Q2: How many ATP can you find?'''
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'''Q3: How many phosphates atoms (orange) does ATP have, and how does this differ to ADP?'''
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'''Q3: What is the location and role of the FO region?'''
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'''Q4: Between which atoms is the high energy bond formed, and in which location in the ATP synthase does the catalysis occur (which chain)?'''
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ATP synthase is an example of a molecular motor.
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'''The F0 region'''
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Use the Structure to answer the questions below.
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<scene name='78/781973/F0/1'>The F0</scene> is a circular rotor that is formed of transmembrane α-helices located in the inner mitochondrial membrane. The positively charged hydrogen ions (protons) travel around the circular F0 motor, and turning the F0 rotor in the process, much like a waterwheel. Firstly, the hydrogen ion binds a negatively charged <scene name='78/781973/Aspgluchain/1'>aspartic acid or glutamic acid</scene> residue (amino acid) within the transmembrane α-helices of the F0 motor. This action then allows the F0 to turn, as it can only turn in the hydrophobic membrane when a hydrogen ion is bound to these amino acids, as it neutralises the amino acids negative charge. Secondly, after a full rotation, the hydrogen is removed from the rotor by an <scene name='78/781973/Arg/1'>arginine</scene> amino acid, into a charged pocket, and then is passed to the opposite side of the membrane.
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'''Q4: How many phosphates does ATP have?'''
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'''Q5: What is the location and role of the F0 region. How many Transmembrane α-helices are there?'''
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'''Q5: What would be the xxxxxx'''
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'''Q6: Name two key amino acids, one acidic and one basic, that influence the hydrogen ions's path within the the F0. Which one acts like a broom sweeping the protons off the rotor?'''
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'''Summary'''
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The synthesis of ATP, the cells energy currency, involves a number of steps performed by a tiny molecular motor found in the mitochondrial membrane, called ATP synthase.
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'''Key Terms'''
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ATP = Adenosine triphosphate (nucleotide)
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ADP = Adenosine diphosphate (nucleotide)
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Aspartic acid = An acidic amino acid (negatively charged)
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Glutamic acid = An acidic amino acid (negatively charged)
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Arginine = A basic amino acid (positively charged)
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Transmembrane α-helices = Membrane-spanning α-helices
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ATP synthase = A molecular motor that generates ATP
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Hydrogen ion = A hydrogen atom that has lost (or gained) an electron. A positively charged hydrogen ion is also referred to as a proton
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Moiety = A "part" or "functional group" of a molecule
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You were viewing the molecular model using the Jmol viewer within [http://proteopedia.org/wiki/index.php/Main_Page Proteopedia].
</StructureSection>
</StructureSection>

Current revision

ATP Synthase

ATP Synthase (PDB entry 5lqz)

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Proteopedia Page Contributors and Editors (what is this?)

Alice Clark

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