Fig. 2: Structure of the isolated Vo domain.
From: Rotary mechanism of the prokaryotic Vo motor driven by proton motive force
A The density map of the isolated Vo domain. The map is colored according to the local resolution (see key). Left: overall structure. Right: the cross-section image of the region is indicated by the dotted lines in the left panel. B The salt bridge formed between a/R563, a/R622, and c/E63. The residues are shown as sticks. The density maps are shown as semi-transparent. The scale bar shows 3 Å. The left panel represents a comparison of the salt bridge structure of isolated Vo and Vo in the holo-enzyme. The superimposed image of the salt bridge of the isolated Vo (colored) and the Vo domain of holo-enzyme (gray). C The angles adopted by the c/E63 residues. The dashed semi-circle indicates the circumference of the c12-ring. The red lines indicate the angle of the E63 side chain of each c-subunit. The scale bar shows 10 Å. The insets are the magnified views of the regions indicated by the dotted rectangles. The scale bar shows 5 Å. D Plot of the angles of c/E63.
