Stabilization of Fo/Vo/Ao by a radial electric field
- PMID: 27857597
- PMCID: PMC5036770
- DOI: 10.2142/biophysics.7.99
Stabilization of Fo/Vo/Ao by a radial electric field
Abstract
The membrane domain of rotary ATPases (Fo/Vo/Ao) contains a membrane-embedded rotor ring which rotates against an adjacent cation channel-forming subunit during catalysis. The mechanism that allows stabilization of the highly mobile and yet tightly connected domains during operation while not impeding rotation is unknown. Remarkably, all known ATPase rotor rings are filled by lipids. In the crystal structure of the rotor ring of a V-ATPase from Enterococcus hirae the ring filling lipids form a proper membrane that is lower with respect to the embedding membrane surrounding both subunits. I propose first, that a vertical shift between lumenal lipids and embedding outside membrane is a general feature of rotor rings and second that it leads to a radial potential fall-off between rotor ring and cation channel, creating attractive forces that impact rotor-stator interaction in Fo/Vo/Ao during rotation.
Keywords: ATP synthase; electrochemical gradient; membrane protein; transmembrane electric field.
Figures




Similar articles
-
How does transmembrane electrochemical potential drive the rotation of Fo motor in an ATP synthase?Protein Cell. 2015 Nov;6(11):784-91. doi: 10.1007/s13238-015-0217-6. Protein Cell. 2015. PMID: 26472431 Free PMC article.
-
Molecular structure and rotary dynamics of Enterococcus hirae V₁-ATPase.IUBMB Life. 2014 Sep;66(9):624-30. doi: 10.1002/iub.1311. Epub 2014 Sep 17. IUBMB Life. 2014. PMID: 25229752 Review.
-
Off-axis rotor in Enterococcus hirae V-ATPase visualized by Zernike phase plate single-particle cryo-electron microscopy.Sci Rep. 2018 Oct 23;8(1):15632. doi: 10.1038/s41598-018-33977-9. Sci Rep. 2018. PMID: 30353110 Free PMC article.
-
Six states of Enterococcus hirae V-type ATPase reveals non-uniform rotor rotation during turnover.Commun Biol. 2023 Jul 28;6(1):755. doi: 10.1038/s42003-023-05110-8. Commun Biol. 2023. PMID: 37507515 Free PMC article.
-
Structural model of the transmembrane Fo rotary sector of H+-transporting ATP synthase derived by solution NMR and intersubunit cross-linking in situ.Biochim Biophys Acta. 2002 Oct 11;1565(2):232-45. doi: 10.1016/s0005-2736(02)00572-2. Biochim Biophys Acta. 2002. PMID: 12409198 Review.
Cited by
-
Essay on Biomembrane Structure.J Membr Biol. 2019 Jun;252(2-3):115-130. doi: 10.1007/s00232-019-00061-w. Epub 2019 Mar 15. J Membr Biol. 2019. PMID: 30877332 Free PMC article. Review.
-
Two-dimensional crystallization of intact F-ATP synthase isolated from bovine heart mitochondria.Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Dec;69(Pt 12):1368-70. doi: 10.1107/S1744309113029072. Epub 2013 Nov 29. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013. PMID: 24316832 Free PMC article.
References
-
- Boyer P. The ATP synthase-a splendid molecular machine. Annu Rev Biochem. 1997;66:717–49. - PubMed
-
- Wilkens S. Rotary molecular motors. Adv Protein Chem. 2005;71:345–82. - PubMed
-
- Junge W, Sielaff H, Engelbrecht S. Torque generation and elastic power transmission in the rotary F(o)F(1)-ATPase. Nature. 2009;459:364–70. - PubMed
-
- Noji H, Yasuda R, Yoshida M, Kinosita K. Direct observation of the rotation of F1-ATPase. Nature. 1997;386:299–302. - PubMed
LinkOut - more resources
Full Text Sources