PDBsum entry 6b8h

Membrane protein

PDB id: 6b8h

Contents

Protein chains

(+ 14 more) 75 a.a.

48 a.a.

249 a.a.

200 a.a.

157 a.a.

49 a.a.

84 a.a.

106 a.a.

59 a.a.

24 a.a.

(+ 0 more) 501 a.a.

(+ 0 more) 470 a.a.

265 a.a.

119 a.a.

48 a.a.

161 a.a.

21 a.a.

Ligands

ANP ×10

Metals

_MG ×10

References listed in PDB file

Key reference

• Title: Atomic model for the dimeric f_oregion of mitochondrial ATP synthase.
• Authors: H.Guo, S.A.Bueler, J.L.Rubinstein.
• Ref.: Science, 2017, 358, 936-940. [DOI no: 10.1126/science.aao4815]
• PubMed id: 29074581

Abstract

Mitochondrial adenosine triphosphate (ATP) synthase produces the majority of ATP in eukaryotic cells, and its dimerization is necessary to create the inner membrane folds, or cristae, characteristic of mitochondria. Proton translocation through the membrane-embedded F_Oregion turns the rotor that drives ATP synthesis in the soluble F₁region. Although crystal structures of the F₁region have illustrated how this rotation leads to ATP synthesis, understanding how proton translocation produces the rotation has been impeded by the lack of an experimental atomic model for the F_Oregion. Using cryo-electron microscopy, we determined the structure of the dimeric F_Ocomplex fromSaccharomyces cerevisiaeat a resolution of 3.6 angstroms. The structure clarifies how the protons travel through the complex, how the complex dimerizes, and how the dimers bend the membrane to produce cristae.