PART TWO: ATP Synthase Before you work on this part of the assignment, prepare b
ID: 204086 • Letter: P
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PART TWO: ATP Synthase Before you work on this part of the assignment, prepare by reading your textbook. In addition, the following video might help you to visualize the overall process of ATP synthesis http://www.sumanasinc.com/webcontent/animations/content/atpsynthase html The actual assignment (15 points) Go to the following webpage of the Online Macromolecular Museum Exhibits and explore the structure and function of ATP synthase: http://earth.callutheran.edu/Academic Programs/Departments/BioDev/omm/ismolnew/atp_synthase/ atp synthase.html Follow the instructions of this web-page. As you click on the round buttons, the structural display ATPase will change. The text and the exhibit, you will encounter the structural displays shown in the figures of this assign of structure are always color coordinated. As you work through this ment Figure 1: Which subunit is shown here? One residue is highlighted in red. What is the name of the red residue and what is its functional significance? Figure 2: What are the names of the purple and golden-brown colored parts? Which part rotates? What is the consequence of this rotation for the other part? Figure 3: What happens inside the conformers LOOSE, OPEN, and TIGHT of the beta subunits of the F1 complex? OPENExplanation / Answer
Fig 1. Aspartate 61 is highlighted in red. Its main function is in rotation of c ring as Asp 61 residue's sidechain are capable of protonation and deprotonation.
Fig 2. Purple colour represent central Stalk (it has delta, epsilon and gamma subunits) and golden brown represents catalytic complex (have 3 alpha subunit and 3 beta subunits).
Catalytic complex( beta subunits) rotates.
As we know that beta subunits of catalytic complex rotates which help in releasing of ATP, as there is a conformational changes due to rotation.
Fig 3. As we know that due to rotation there is conformational changes in beta subunits so it has 3 conformers 1. Loose, 2. Tight and 3. Open. Beta subunits sequentially cycles in these three conformers L---> T ---> O. The LOOSE conformation allows
the loose binding of ADP and Pi substrates, but is unable to catalysis ATP formation. The TIGHT conformation forms ATP (ADP + Pi ---> ATP) but unable to release ATP. When conformatiom from TIGHT to OPEN change then only it can release ATP.
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