Figure 8 - full size

 

Figure 8.
Figure 8 Changes in the solvent-accessible surface (a) for the N1/N2 interface in the lactoferrin N-lobe and (b) for the N-lobe/C-lobe interface. In each case the open ApoLf structure is on the left and the closed Fe[2]Lf structure is on the right. Surface area buried between N1 and N2 domains is much larger in the closed form (a, right panel). On the other hand, the surface area buried between the N- and C-lobes is greater in the open form (b, left panel). In (a) the N2 domain surface is white and the N1 domain surface is magenta; only the portions of the surface that come into contact (within 4.5 Å) are shown. The much larger contact surface for the closed form (a, right) arises because the N2 domain (upper) rotates over the N1 domain (lower) about an axis running left to right across the page. In (b) the N-lobe surface is magenta and the C-lobe surface is white. The greater contact area between the lobes in the open form (left) arises because of the movement of the N2 domain (upper, left) up against the connecting helix (H12) and the C-lobe. The rotation axis is approximately about an axis running top to bottom across the page. Figure prepared with GRASP (Nicholls et al., 1993[Nicholls, A., Bharadwaj, R. & Honig, B. (1993). Biophys. J. 64, 166.]).

The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1998, 54, 1319-1335) copyright 1998.