Crystal structures of mutant forms of the yeast F1 ATPase reveal two modes of uncoupling.
J Biol Chem
; 285(47): 36561-9, 2010 Nov 19.
Article
in En
| MEDLINE
| ID: mdl-20843806
ABSTRACT
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(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 γLeu83 and ß(DP) residues, Leu-391 and Glu-395, located in Catch 2 region, is reduced allowing rotation of the γ-subunit with less impedance. Overall, the structures provide key insights into the critical interactions in the yeast ATP synthase involved in the coupling process.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Saccharomyces cerevisiae
/
Proton-Translocating ATPases
/
Mutant Proteins
/
Mutation
Type of study:
Prognostic_studies
Language:
En
Journal:
J Biol Chem
Year:
2010
Type:
Article
Affiliation country:
United States