Abstract
Lens-specific aquaporin-0 (AQP0) functions as a specific water pore and forms the thin junctions between fiber cells in the lens. We describe a 1.9 Å 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 N- and C-termini. The pore in junctional AQP0 appears to be closed and retains only three water molecules in the center of the pore, 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. This made it possible to build an atomic model for the lipid bilayer surrounding the AQP0 tetramers and to describe non-specific lipid-protein interactions.
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