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Alice Clark/ATPsynthase
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<StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'> | <StructureSection load='5lqz' size='350' side='right' caption='ATP Synthase (PDB entry [[5lqz]])' scene='78/781973/Start/1'> | ||
| - | ATP synthase is shown here to the right in 3D with each protein shown in a different colour. | + | ATP synthase is shown here to the right ==> |
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| + | It is depicted in 3D with each protein shown in a different colour. | ||
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Tools for exploring ATP synthase in 3D | Tools for exploring ATP synthase in 3D | ||
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- green text - click to load a new 3D scene | - green text - click to load a new 3D scene | ||
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'''Have a go yourself now ==>''' | '''Have a go yourself now ==>''' | ||
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| - | '''The | + | '''The F1 and Axle''' |
| - | The <scene name='78/781973/Alpha-beta/1'>F1 motor head</scene> contains 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>, | + | 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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'''ADP and ATP are bound in the nucleotide binding sites''' | '''ADP and ATP are bound in the nucleotide binding sites''' | ||
| - | 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 | + | 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. ==> |
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. | 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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| - | '''The F0 region | + | '''The F0 region''' |
| - | <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 | + | <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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| - | '''Q5: What is the location and role of the | + | '''Q5: What is the location and role of the F0 region. How many Transmembrane α-helices are there?''' |
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| - | '''Q6: Name two key amino acids, one acidic and one basic, that | + | '''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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'''Key Terms''' | '''Key Terms''' | ||
| - | ATP = | + | ATP = Adenosine triphosphate (nucleotide) |
| - | ADP = | + | ADP = Adenosine diphosphate (nucleotide) |
| - | Aspartic acid = | + | Aspartic acid = An acidic amino acid (negatively charged) |
| - | Glutamic acid = | + | Glutamic acid = An acidic amino acid (negatively charged) |
| - | Arginine = | + | Arginine = A basic amino acid (positively charged) |
| - | Transmembrane α-helices = | + | Transmembrane α-helices = Membrane-spanning α-helices |
| - | ATP synthase | + | ATP synthase = A molecular motor that generates ATP |
Hydrogen ion = A hydrogen atom that has lost (or gained) an electron. A positively charged hydrogen ion is also referred to as a proton | 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 | ||
Current revision
ATP Synthase
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