Structural highlights
Function
[ATPL_ECOLI] F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. 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.[HAMAP-Rule:MF_01396] Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of 10 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.[HAMAP-Rule:MF_01396]
Evolutionary Conservation
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Publication Abstract from PubMed
F1F0 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 F0 portion drives these catalytic changes is less clear. Here we describe the structural changes in the proton-translocating F0 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 F0 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.
Structural changes linked to proton translocation by subunit c of the ATP synthase.,Rastogi VK, Girvin ME Nature. 1999 Nov 18;402(6759):263-8. PMID:10580496[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rastogi VK, Girvin ME. Structural changes linked to proton translocation by subunit c of the ATP synthase. Nature. 1999 Nov 18;402(6759):263-8. PMID:10580496 doi:http://dx.doi.org/10.1038/46224
