| Type: | Domain | Name: | Skp domain |
| Description: | This entry represents the Skp (also known as OmpH) domain, named after the Skp protein which functions as a periplasmic chaperone for newly synthesised outer-membrane proteins [, ]. Three hairpin-shaped alpha-helical extensions reach out by approximately 60 A from a trimerisation region, which is composed of three intersubunit beta-sheets that wind around a central axis. The alpha-helical extensions approach each other at their distal turns, resulting in a fold that resembles a 'three-pronged grasping forcep'. The overall shape of Skp is reminiscent of the cytosolic chaperone prefoldin (), although it is based on a radically different topology. The peculiar architecture, with apparent plasticity of the prongs and distinct electrostatic and hydrophobic surface properties, supports the recently proposed biochemical mechanism of this chaperone: formation of a Skp(3)-Omp complex protects the outer membrane protein from aggregation during passage through the bacterial periplasm. | Short Name: | Skp_domain |
