Lipid–protein interactions in double- layered two-dimensional.pdfVIP

Vol 438|1 December 2005 |doi:10.1038/nature04321 ARTICLES Lipid–protein interactions in double- layered two-dimensional AQP0 crystals 1 1 2,3 4 4 2,3 Tamir Gonen , Yifan Cheng , Piotr Sliz , Yoko Hiroaki , Yoshinori Fujiyoshi , Stephen C. Harrison Thomas Walz1 Lens-specific aquaporin-0 (AQP0) functions as a specific water pore and forms the thin junctions between fibre cells. ˚ Here we describe a 1.9 A resolution structure of junctional AQP0, determined by electron crystallography of double- layered two-dimensional crystals. Comparison of junctional and non-junctional AQP0 structures shows that junction formation depends on a conformational switch in an extracellular loop, which may result from cleavage of the cytoplasmic amino and carboxy termini. In the centre of the water pathway, the closed pore in junctional AQP0 retains only three water molecules, which are too widely spaced to form hydrogen bonds with each other. Packing interactions between AQP0 tetramers in the crystalline array are mediated by lipid molecules, which assume preferred conformations. We were therefore able to build an atomic model for the lipid bilayer surrounding the AQP0 tetramers, and we describe lipid–protein interactions. Members of the aquaporin (AQP) family form membrane pores emission gun and a 4,096-pixel £ 4,096-pixel charge-coupled device that are either highly selective for water (aquaporins) or also camera, we have now been able to collect electron diffraction data to permeable to other small neutral solutes such as glycerol and urea much higher resolution. (aquaglyceroporins) (reviewed