Crystal Structures of Mutant Forms of the Yeast F[subscript 1] ATPase Reveal Two Modes of Uncoupling
- Rosalind
The mitochondrial ATP synthase couples the flow of protons with the phosphorylation of ADP. A class of mutations, the mitochondrial genome integrity (mgi) mutations, has been shown to uncouple this process in the yeast mitochondrial ATP synthase. Four mutant forms of the yeast F{sub 1} ATPase with mgi mutations were crystallized; the structures were solved and analyzed. The analysis identifies two mechanisms of structural uncoupling: one in which the empty catalytic site is altered and in doing so, apparently disrupts substrate (phosphate) binding, and a second where the steric hindrance predicted between {gamma}Leu83 and {beta}{sub DP} residues, Leu-391 and Glu-395, located in Catch 2 region, is reduced allowing rotation of the {gamma}-subunit with less impedance. Overall, the structures provide key insights into the critical interactions in the yeast ATP synthase involved in the coupling process.
- Research Organization:
- Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Sponsoring Organization:
- USDOE
- OSTI ID:
- 1002871
- Journal Information:
- J. Biol. Chem., Vol. 285, Issue 09, 2010; ISSN 0021-9258
- Country of Publication:
- United States
- Language:
- ENGLISH
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