2B6O

Electron crystallographic structure of lens Aquaporin-0 (AQP0) (lens MIP) at 1.9A resolution, in a closed pore state

Summary for 2B6O

• Entry DOI: 10.2210/pdb2b6o/pdb
• Related: 1SOR 1YMG 2B6P
• Descriptor: Lens fiber major intrinsic protein, 1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE (3 entities in total)
• Functional Keywords: aquaporin-0 junctions, aqp0, lens mip, lipid-protein interactions, membrane, lipid bilayer, closed water pore, membrane protein
• Biological source: Ovis aries (sheep)
• Total number of polymer chains: 1
• Total formula weight: 34386.28

Authors

Gonen, T.,Cheng, Y.,Sliz, P.,Hiroaki, Y.,Fujiyoshi, Y.,Harrison, S.C.,Walz, T. (deposition date: 2005-10-03, release date: 2005-12-06, Last modification date: 2023-08-23)

Primary citation

Gonen, T.,Cheng, Y.,Sliz, P.,Hiroaki, Y.,Fujiyoshi, Y.,Harrison, S.C.,Walz, T.
Lipid-protein interactions in double-layered two-dimensional AQP0 crystals.
Nature, 438:633-638, 2005

PubMed Abstract: 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.

PubMed: 16319884
DOI: 10.1038/nature04321

Experimental method

ELECTRON CRYSTALLOGRAPHY (1.9 Å)