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Cryo-EM structures provide insight into how E. coli F1Fo ATP synthase accommodates symmetry mismatch
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Cryo-EM structures provide insight into how E. coli F1Fo ATP synthase accommodates symmetry mismatch
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Journal Article
Cryo-EM structures provide insight into how E. coli F1Fo ATP synthase accommodates symmetry mismatch
2020
Overview
F
1
F
o
ATP synthase functions as a biological rotary generator that makes a major contribution to cellular energy production. It comprises two molecular motors coupled together by a central and a peripheral stalk. Proton flow through the F
o
motor generates rotation of the central stalk, inducing conformational changes in the F
1
motor that catalyzes ATP production. Here we present nine cryo-EM structures of
E. coli
ATP synthase to 3.1–3.4 Å resolution, in four discrete rotational sub-states, which provide a comprehensive structural model for this widely studied bacterial molecular machine. We observe torsional flexing of the entire complex and a rotational sub-step of F
o
associated with long-range conformational changes that indicates how this flexibility accommodates the mismatch between the 3- and 10-fold symmetries of the F
1
and F
o
motors. We also identify density likely corresponding to lipid molecules that may contribute to the rotor/stator interaction within the F
o
motor.
F
1
F
o
ATP synthase consists of two coupled rotary molecular motors: the soluble ATPase F
1
and the transmembrane F
o
. Here, the authors present cryo-EM structures of
E. coli
ATP synthase in four discrete rotational sub-states at 3.1-3.4 Å resolution and observe a rotary sub-step of the F
o
motor cring that reveals the mechanism of elastic coupling between the two rotary motors, which is essential for effective ATP synthesis.
