STRUCTURE OF THE SUCROSE-SPECIFIC PORIN SCRY FROM SALMONELLA-TYPHIMURIUM AND ITS COMPLEX WITH SUCROSE

The X-ray structure of a sucrose-specific porin (ScrY) from Salmonella typhimurium has been determined by multiple isomorphous replacement a t 2.4 Angstrom resolution both in its uncomplexed form and with bound sucrose. ScrY is a noncrystallographic trimer of identical subunits, e ach with 413 structurally well-defined amino acids. A monomer is built up of 18 anti-parallel beta-strands surrounding a hydrophilic pore, w ith a topology closely similar to that of maltoporin. Two non-overlapp ing sucrose-binding sites were identified in difference Fourier maps. The higher permeability for sucrose of ScrY as compared to maltoporin is mainly accounted for by differences in their pore-lining residues.