![Perspective ,[object Object],[object Object],[object Object],[object Object],1937 1961 1964 1981 1994 1997 Herman Kalckar (Denmark) links ATP synthase is linked with cell respiration The American Ephraim Racker isolates the F1 part of the ATP synthase. Peter Mitchell (UK) shows that cell respiration leads to pH change inside and outside the mitochondrial membrane John E. Walker determines the DNA sequence of the genes encoding the proteins in ATP synthase. Walker and coworkers determine The structure of the F1 part of the ATP synthase ATP synthase rotate during the synthesis and hydrolysis of ATP is demonstrated by Richard Cross (USA) Wolfgang Junge (Germany) and Masasuke Yoshida (Japan)](data:image/gif;base64,R0lGODlhAQABAIAAAAAAAP///yH5BAEAAAAALAAAAAABAAEAAAIBRAA7)
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ATP-Synthase Presentation
- 1. Molecular Architecture of the Rotary Motor in ATP Synthase Ahmed Ibrahim Structure and Function Relationships of Membrane Proteins November 14, 2006 Daniela Stock, Andrew G. W. Leslie, John E. Walker
- 8. 120 ° goes through one of three subunit pair (full circle)
- 10. 1. All species contain three domains in the F 0 subunit: a, b, and c 2. In E. coli the stoichiometry of these subunits is a1:b2:c9-11 3. Cross-linking and genetic experiments have shown that there are 12 c subunits per F 0 4. Biochemical and mutational experiments have shown that the a and c subunits contain functional groups that are necessary for proton translocation through the membrane. 6. Nuclear Magnetic Resonance (NMR) has shown the structure of a c subunit as two alpha-helices linked by an extra-membrane loops. Current Data on F 0 of ATP Synthase Composition
- 11. Nuclear Magnetic Resonance (NMR)-derived Structure of the c Subunit of the F 0 Portion of ATP Synthase Mutational (truncation) studies in Saccharomyces cerevisiae have shown that Asp61 in E. coli and Glu59 at the COOH end of the c subunit is necessary for proton translocation
- 14. Approach of the Study 1. Purified ATP synthase from Sacchromyces Cervesiae (yeast) and performed crystallization experiments. 2. Yeast ATP synthase after analysis with SDS page and HPLC found 13 subunits for ATP synthase: F 1 : α , β , γ , ε , δ F 0 : a, b, c, d , h , f , OSCP , and ATP8
- 18. 1. The 10 c subunits form an almost symmetrical ring. 2. density for subunits 6, 7, and 8 is weaker, as seen from the asymmetrical appearance of the electron density 3. Increased density in the upper two thirds is probably due to phospholipids occupancy.
- 21. The electron density shown provides evidence that c protomers form a ring that is in close contact with the γ and δ subunits. Consistent with previous interpretations, in which subunits γ , δ , and ε form a rotating ensemble. It strongly supports the idea that the c oligomer is part of a rotary motor, converting electrochemical energy into chemical energy stored in ATP.
- 22. To understand the mechanism of the generation of rotation (FUNCTION) , it will be necessary to establish the nature of the interaction between the c subunit oligomer (Structure) found here and the remaining subunits in F0. Conclusion