Fig. 5: MgATP induced ε-subunit rearrangements in P. aeruginosa ATP synthase. | Nature Communications

Fig. 5: MgATP induced ε-subunit rearrangements in P. aeruginosa ATP synthase.

From: Distinct structural features of Pseudomonas aeruginosa ATP synthase revealed by cryo-electron microscopy

Fig. 5

Cryo-EM analysis of P. aeruginosa ATP synthase after incubation with 10 mM MgATP yielded multiple maps, capturing the enzyme in distinct rotary and inhibitory states (Fig. S7). Two maps of the enzyme in rotary State 2 are shown here, illustrating different conformations of the inhibitory ε subunit. Left: autoinhibited “up” extended state, preventing rotation. Right: active “down” condensed state, allowing the rotation of the γ subunit. Cryo-EM maps colored as in previous figures, with non-protein density transparent, and close-up views of the εCTD with helices labelled.

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