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Structural changes linked to proton translocation by subunit c of the ATP synthase

Nature volume 402, pages 263–268 (1999)Cite this article

Abstract

F1FO ATP synthases use a transmembrane proton gradient to drive the synthesis of cellular ATP. The structure of the cytosolic F1 portion of the enzyme and the basic mechanism of ATP hydrolysis by F1 are now well established, but how proton translocation through the transmembrane FO portion drives these catalytic changes is less clear. Here we describe the structural changes in the proton-translocating FO subunit c that are induced by deprotonating the specific aspartic acid involved in proton transport. Conformational changes between the protonated and deprotonated forms of subunit c provide the structural basis for an explicit mechanism to explain coupling of proton translocation by FO to the rotation of subunits within the core of F1. Rotation of these subunits within F1 causes the catalytic conformational changes in the active sites of F1 that result in ATP synthesis.

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Figure 1: Schematic diagram of F1FO ATP synthase.
Figure 2: Portions of a 3D 1H13C NOESY–heteronuclear single quantum coherence (HSQC) spectrum of subunit c at pH 8, and summary of observed NOEs.
Figure 3: Structure of subunit c at pH 8 and comparison with the structure at pH 5.
Figure 4: Models for the c12 and ac12 subcomplexes of FO.
Figure 5: Proton translocation pathways and model for the functioning complex.

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Acknowledgements

We thank S. Cahill for assistance with the NMR experiments, and M. Brenowitz and V. Schramm for critical reading and discussion of the manuscript.

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  1. Biochemistry Department, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, 10461, New York, USA

    Vinit K. Rastogi & Mark E. Girvin

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Correspondence to Mark E. Girvin.

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Rastogi, V., Girvin, M. Structural changes linked to proton translocation by subunit c of the ATP synthase. Nature 402, 263–268 (1999). https://doi.org/10.1038/46224

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