6vwk

Structural highlights

Function

[F4TL55_ECOLX] 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 between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.[HAMAP-Rule:MF_01396] [C3SL77_ECOLX] Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane.[HAMAP-Rule:MF_01393][RuleBase:RU000483] [D6IFY0_ECOLX] Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0).[HAMAP-Rule:MF_01398][SAAS:SAAS00535352] 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_01398][SAAS:SAAS00002149]

References

1. ↑ Sobti M, Walshe JL, Wu D, Ishmukhametov R, Zeng YC, Robinson CV, Berry RM, Stewart AG. Cryo-EM structures provide insight into how E. coli F1Fo ATP synthase accommodates symmetry mismatch. Nat Commun. 2020 May 26;11(1):2615. doi: 10.1038/s41467-020-16387-2. PMID:32457314 doi:http://dx.doi.org/10.1038/s41467-020-16387-2