Literature DB >> 25168468

Cardiolipin interaction with subunit c of ATP synthase: solid-state NMR characterization.

Ségolène Laage1, Yisong Tao2, Ann E McDermott3.   

Abstract

The interaction of lipids with subunit c from F1F0 ATP synthase is studied by biophysical methods. Subunit c from both Escherichia coli and Streptococcus pneumoniae interacts and copurifies with cardiolipin. Solid state NMR data on oligomeric rings of F0 show that the cardiolipin interacts with the c subunit in membrane bilayers. These studies offer strong support for the hypothesis that F0 has specific interactions with cardiolipin.
Copyright © 2014. Published by Elsevier B.V.

Entities:  

Keywords:  ATP synthase; Cardiolipin; Lipid-protein interaction; Solid-state NMR

Mesh：

Substances：

Year:  2014        PMID： 25168468      PMCID： PMC5526087          DOI： 10.1016/j.bbamem.2014.08.021

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN： 0006-3002


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