Figure 5
Surface-charge distribution of the solved internalin structures. Positive charge is in blue and negative in red. The proteins are not drawn to scale. (a) The concave surface-charge distribution of internalins A, B, C and H, showing the highly negatively charged concave binding pocket seen in all four members of the internalin family. This concave region has been shown to be the binding cleft for internalin A and its receptor E-cadheirin. (b) The convex side of the leucine-rich repeat domain, showing a more neutral and basic surface charge, except for InlB, which has a rather negative overall surface charge. The cap regions of InlA, C and H are comparatively positive, with scattered negative charges on the Ig-like domains. |