Figure 7: Structure of the Pi-bound V1 complex (1PiV1). | Nature Communications

Figure 7: Structure of the Pi-bound V1 complex (1PiV1).

From: Crystal structures of the ATP-binding and ADP-release dwells of the V1 rotary motor

Figure 7

(a) Side view. (b) Top views of the C-terminal domain (transparent surface in a) from the cytoplasmic side in which the ‘bound’ form is superimposed onto that of eV1 (grey). (c) Magnified nucleotide-binding site of the ‘tight’ form in 1PiV1, as in Fig. 4a. The |Fo|-|Fc| maps calculated without Pi:Mg2+ at the binding pockets contoured at 4.0 sigma are shown in red (negative) and green (positive), respectively. (d,e) The viewing position, colours and representations of the binding sites correspond to those in the right panel of c. The ‘tight’ form (c) in 1PiV1, in which the Eh-A residues (67–593) are superimposed onto the same residues of the ‘tight’ form (shown in transparent grey) in eV1 (d) and bV1 (e), as in Fig. 4c. The bound Pi molecule is depicted in stick format and coloured orange.

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