4B2Q

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

4B2Q の概要

• エントリーDOI: 10.2210/pdb4b2q/pdb
• 関連するPDBエントリー: 1VZS 2BO5 2CLY 2WPD 2WSS 2XOK 3ZRY
• EMDBエントリー: 2161
• 分子名称: ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL, ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL, ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL, ... (15 entities in total)
• 機能のキーワード: hydrolase, subtomogram average
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); 詳細
• 細胞内の位置: Mitochondrion inner membrane : P07251 P07251; Mitochondrion: P13620 P02721 P13621 P00830 P00830 P38077 Q12165 P21306 P13619; Mitochondrion membrane ; Multi- pass membrane protein : P61829
• タンパク質・核酸の鎖数: 46
• 化学式量合計: 981278.86

構造登録者

Davies, K.M.,Kuehlbrandt, W. (登録日: 2012-07-17, 公開日: 2012-08-29, 最終更新日: 2024-05-08)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (37 Å)