ENERGY PROFILE OF MALTOOLIGOSACCHARIDE PERMEATION THROUGH MALTOPORIN AS DERIVED FROM THE STRUCTURE AND FROM A STATISTICAL-ANALYSIS OF SACCHARIDE-PROTEIN INTERACTIONS

The crystal structure of the maltodextrin-specific porin from Salmonel la typhimurium ligated with a maltotrioside at the pore eyelet is know n at 2.4 Angstrom resolution. The three glucose units assume a conform ation close to the natural amylose helix. The pore eyelet fits exactly the cross-section of a maltooligosaccharide chain and thus functions as a constraining orifice. The oligomer permeates the membrane by scre wing along the amylose helix through this orifice. Because each glucos e glides along the given helix, its interactions can be sampled at any point along the pathway. The interactions are mostly hydrogen bonds, but also contacts to aromatic rings at one side of the pore. We have d erived the energy profile of a gliding maltooligosaccharide by followi ng formation and breakage of hydrogen bonds and by assessing the sacch aride-aromatics interactions from a statistical analysis of saccharide binding sites in proteins. The resulting profile indicates smooth per meation despite extensive hydrogen bonding at the orifice.