4B2Q

Model of the yeast F1Fo-ATP synthase dimer based on subtomogram average

Summary for 4B2Q

• Entry DOI: 10.2210/pdb4b2q/pdb
• Related: 1VZS 2BO5 2CLY 2WPD 2WSS 2XOK 3ZRY
• EMDB information: 2161
• Descriptor: ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL, ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL, ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL, ... (15 entities in total)
• Functional Keywords: hydrolase, subtomogram average
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Cellular location: Mitochondrion inner membrane : P07251 P07251; Mitochondrion: P13620 P02721 P13621 P00830 P00830 P38077 Q12165 P21306 P13619; Mitochondrion membrane ; Multi- pass membrane protein : P61829
• Total number of polymer chains: 46
• Total formula weight: 981278.86

Authors

Davies, K.M.,Kuehlbrandt, W. (deposition date: 2012-07-17, release date: 2012-08-29, Last modification date: 2024-05-08)

Primary citation

Davies, K.M.,Anselmi, C.,Wittig, I.,Faraldo-Gomez, J.D.,Kuhlbrandt, W.
Structure of the Yeast F1Fo-ATP Synthase Dimer and its Role in Shaping the Mitochondrial Cristae.
Proc.Natl.Acad.Sci.USA, 109:13602-, 2012

PubMed Abstract: We used electron cryotomography of mitochondrial membranes from wild-type and mutant Saccharomyces cerevisiae to investigate the structure and organization of ATP synthase dimers in situ. Subtomogram averaging of the dimers to 3.7 nm resolution revealed a V-shaped structure of twofold symmetry, with an angle of 86° between monomers. The central and peripheral stalks are well resolved. The monomers interact within the membrane at the base of the peripheral stalks. In wild-type mitochondria ATP synthase dimers are found in rows along the highly curved cristae ridges, and appear to be crucial for membrane morphology. Strains deficient in the dimer-specific subunits e and g or the first transmembrane helix of subunit 4 lack both dimers and lamellar cristae. Instead, cristae are either absent or balloon-shaped, with ATP synthase monomers distributed randomly in the membrane. Computer simulations indicate that isolated dimers induce a plastic deformation in the lipid bilayer, which is partially relieved by their side-by-side association. We propose that the assembly of ATP synthase dimer rows is driven by the reduction in the membrane elastic energy, rather than by direct protein contacts, and that the dimer rows enable the formation of highly curved ridges in mitochondrial cristae.

PubMed: 22864911
DOI: 10.1073/PNAS.1204593109

Experimental method

ELECTRON MICROSCOPY (37 Å)