Cryo-EM structures of the autoinhibited <i>E. coli</i> ATP synthase in three rotational states.

ABSTRACT: A molecular model that provides a framework for interpreting the wealth of functional information obtained on the E. coli F-ATP synthase has been generated using cryo-electron microscopy. Three different states that relate to rotation of the enzyme were observed, with the central stalk's ε subunit in an extended autoinhibitory conformation in all three states. The F_o motor comprises of seven transmembrane helices and a decameric c-ring and invaginations on either side of the membrane indicate the entry and exit channels for protons. The proton translocating subunit contains near parallel helices inclined by ~30° to the membrane, a feature now synonymous with rotary ATPases. For the first time in this rotary ATPase subtype, the peripheral stalk is resolved over its entire

SUBMITTER: Sobti M 

PROVIDER: S-EPMC5214741 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature