Structural Asymmetry and Kinetic Limping of Single Rotary F-ATP Synthases

Structural Asymmetry and Kinetic Limping of Single Rotary F-ATP Synthases

F-ATP synthases use proton flow through the F<sub>O</sub> domain to synthesize ATP in the F<sub>1</sub> domain. In <i>Escherichia coli</i>, the enzyme consists of rotor subunits γε<b>c</b><sub>10</sub> and stator subunits...

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Bibliographic Details
Main Authors:	Hendrik Sielaff, Seiga Yanagisawa, Wayne D. Frasch, Wolfgang Junge, Michael Börsch
Format:	Article
Language:	English
Published:	MDPI AG 2019-01-01
Series:	Molecules
Subjects:	F<sub>O</sub>F<sub>1</sub> ATP synthase <i>Escherichia coli</i> single-molecule fluorescence symmetry cryo-EM structure subunit rotation elasticity
Online Access:	https://www.mdpi.com/1420-3049/24/3/504

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