3OEH

Structure of four mutant forms of yeast F1 ATPase: beta-V279F

Summary for 3OEH

• Entry DOI: 10.2210/pdb3oeh/pdb
• Related: 1W0J 2HLD 3FKS 3OE7 3OEE 3OFN
• Descriptor: ATP synthase subunit alpha, ATP synthase subunit beta, ATP synthase subunit gamma, ... (7 entities in total)
• Functional Keywords: atp synthase, atp phosphatase, f1f0 atpase, atp synthesis, hydrolase, adp, po4, mitochondria
• Biological source: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast); More
• Cellular location: Mitochondrion inner membrane: P07251; Mitochondrion: P00830 P38077 Q12165 P21306
• Total number of polymer chains: 27
• Total formula weight: 1127068.92

Authors

Arsenieva, D.,Symersky, J.,Wang, Y.,Pagadala, V.,Mueller, D.M. (deposition date: 2010-08-12, release date: 2010-09-15, Last modification date: 2023-09-06)

Primary citation

Arsenieva, D.,Symersky, J.,Wang, Y.,Pagadala, V.,Mueller, D.M.
Crystal structures of mutant forms of the yeast f1 ATPase reveal two modes of uncoupling.
J.Biol.Chem., 285:36561-36569, 2010

PubMed 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 β(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.

PubMed: 20843806
DOI: 10.1074/jbc.M110.174383

Experimental method

X-RAY DIFFRACTION (3 Å)