Structure and Mechanisms of F-Type ATP Synthases: Suppleme

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Play, download and edit the free video Structure and Mechanisms of F-Type ATP Synthases: Supplemental Video 4.

A supplemental video from the 2019 review by Werner Kühlbrandt, "Structure and Mechanisms of F-Type ATP Synthases," from the Annual Review of Biochemistry: annualreviews.org/doi/10.1146/annurev-biochem-013118-110903?utm_source=viemo&utm_medium=bi.kuhlbrandt&utm_campaign=suppvideo

Shown: The δ/OSCP hinge. The N-terminal α-helical domain of the two-domain subunit δ/OSCP (shown here is subunit OSCP of Polytomella mitochondrial ATP synthase) is attached to the F1 head by the N-terminal extensions of two of the three α-subunits (dark green). The C-terminal δ/OSCP domain is attached to the peripheral stalk (gray) by interaction of one OSCP helix with the N-terminal extension of the third α-subunit. Joint rotation of the F1 head with the central stalk for the first part of each ATP-generating power stroke (see Supplemental Video 3) is facilitated by the single-peptide link which connects the two δ/OSCP domains, acting as a hinge. The hinge movement enables flexible coupling of the central rotor and F1 head and overcomes the symmetry mismatch between the near-threefold F1 head and the eight to 17-fold symmetry (tenfold for Polytomella or yeasts; 14-fold for chloroplasts; see Figure 9 and Supplemental Video 5) of the c-ring rotor. Adapted from reference 81.

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