The Structure of G1pF, A Glycerol Conducting Channel

Summary

The passage of water or small neutral solutes across the cell membrane in animals, plants and bacteria is facilitated by a family of homologous membrane channels, variously known as aquaporins though perhaps more correctly as aquaglyceroporins. The glycerol facilitator (G1pF) is a 28 kDa aquaglyceroporin that catalyses transmembrane diffusion of glycerol and certain linear polyhydric alcohols in Escherichia coli. X-ray crystallographic analysis of G1pF to 2.2 Å resolution revealed an α-barrel structure, surrounded by six full-length transmembrane helices and two half-spanning helices that are joined head-to-head in the middle of the membrane. These helices are arranged to a quasi twofold manner relative to the central membrane plane, where highly conserved residues make helix-to-helix contacts that stabilize the relative position and orientation of the helices in the structure. This sequence–structure correlation suggests that the evolutionary divergence of aquaporins and aquaglyceroporins is constrained by a conserved structural framework within which specialized function may be developed. Three glycerol molecules were resolved in the central channel through the G1pF monomer, thereby defining a transmembrane channel for glycerol permeation. The structure of glycerol–G1pF complex provides insight into the chemical basis for transmembrane selective permeability.