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Fig. 4. Electron density corresponding to polyphenol inhibitors bound to bovine F₁-ATPase. (A-C) The (2F_o-F_c) electron density maps contoured at 1s for resveratrol, piceatannol, and quercetin, respectively. In A and C, two binding modes (green and violet carbon skeletons, with red oxygen atoms) are shown for resveratrol and quercetin. In each case, they were assigned occupancies of 75% and 25%, respectively. For quercetin, they correspond to cis and trans isomers, respectively. In B, piceatannol was assigned an occupancy of 100%. (D and E) Each of the bound resveratrol molecules shown in A has two possible orientations produced by rotating the molecule about its long axis. At the resolution of current electron density map, they are indistinguishable.

Fig. 5. Lack of binding pocket for resveratrol and related compounds in the region of the bearing formed between the C-terminal tip of the g-subunit and the b_DP- and b_E-subunits (A and B, respectively). In both parts, the three a-subunits and the two other b-subunits have been removed for clarity.

Fig. 6. Alignments of sequences in regions of the a-, b-, and g-subunits of bovine F₁-ATPase with sequences from the same subunits in selected species. (A-C) sequences from a- b-, and g-subunits, respectively. Asterisks and colons denote identity and extensive conservation of residues, respectively. Arrows indicate the residues that form the resveratrol-binding pocket. In A and B, they are in the a_TP- and b_TP-subunits, and in addition, in A, a_DPGlu-292 also contributes to the site.