3OEH: Structure Of Four Mutant Forms Of Yeast F1 Atpase: Beta-V279f

Citation:
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 gammaLeu83 and beta(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.
PDB ID: 3OEHDownload
MMDB ID: 84903
PDB Deposition Date: 2010/8/12
Updated in MMDB: 2010/12
Experimental Method:
x-ray diffraction
Resolution: 3  Å
Source Organism:
Similar Structures:
Biological Unit for 3OEH: nonameric; determined by author
Molecular Components in 3OEH
Label Count Molecule
Proteins (9 molecules)
3
ATP Synthase Subunit Alpha(Gene symbol: ATP1)
Molecule annotation
3
ATP Synthase Subunit Beta(Gene symbol: ATP2)
Molecule annotation
1
ATP Synthase Subunit Gamma(Gene symbol: ATP3)
Molecule annotation
1
ATP Synthase Subunit Delta(Gene symbol: ATP16)
Molecule annotation
1
ATP Synthase Subunit Epsilon(Gene symbol: ATP15)
Molecule annotation
Chemicals (10 molecules)
1
5
2
5
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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