6b8h
Mosaic model of yeast mitochondrial ATP synthase monomer
Structural highlights
FunctionATP9_YEAST Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element. Publication Abstract from PubMedMitochondrial 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 FO region turns the rotor that drives ATP synthesis in the soluble F1 region. While crystal structures of the F1 region have illustrated how rotation leads to ATP synthesis, the lack of an experimental atomic model for the FO region has prevented understanding how proton translocation produces rotation. We determined the structure of the dimeric FO complex from Saccharomyces cerevisiae at 3.6 A resolution by electron cryomicroscopy. The structure reveals the proton path through the complex, how the complex dimerizes, and suggests how it bends the membrane to produce cristae. Atomic model for the dimeric FO region of mitochondrial ATP synthase.,Guo H, Bueler SA, Rubinstein JL Science. 2017 Oct 26. pii: eaao4815. doi: 10.1126/science.aao4815. PMID:29074581[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
| ||||||||||||||||
