2b6p
From Proteopedia
X-ray structure of lens Aquaporin-0 (AQP0) (lens MIP) in an open pore state
Overview
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.
About this Structure
2B6P is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Lipid-protein interactions in double-layered two-dimensional AQP0 crystals., Gonen T, Cheng Y, Sliz P, Hiroaki Y, Fujiyoshi Y, Harrison SC, Walz T, Nature. 2005 Dec 1;438(7068):633-8. PMID:16319884 Page seeded by OCA on Sat May 3 19:55:31 2008
Categories: Bos taurus | Single protein | Cheng, Y. | Fujiyoshi, Y. | Gonen, T. | Harrison, S C. | Hiroaki, Y. | Sliz, P. | Walz, T. | Aqp0 | Aquaporin | Aquaporin-0 | Lens mip | Membrane protein; | Open water pore
