Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Lipid-protein interactions in double-layered two-dimensional AQP0 crystals.
Journal, issue, pages	Nature, Vol. 438, Issue 7068, Page 633-638, Year 2005
Publish date	Dec 1, 2005
Authors	Tamir Gonen / Yifan Cheng / Piotr Sliz / Yoko Hiroaki / Yoshinori Fujiyoshi / Stephen C Harrison / Thomas Walz /
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 ...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.
External links	Nature / PubMed:16319884 / PubMed Central
Methods	EM (electron crystallography) / X-ray diffraction
Resolution	1.9 - 2.4 Å
Structure data	EMDB-2973: electron crystallographic structure of lens Aquaporin-0 (AQP0) (lens MIP) at 1.9A resolution, in a closed pore state Method: EM (electron crystallography) / Resolution: 1.9 Å PDB-2b6o: Electron crystallographic structure of lens Aquaporin-0 (AQP0) (lens MIP) at 1.9A resolution, in a closed pore state Method: ELECTRON CRYSTALLOGRAPHY / Resolution: 1.9 Å PDB-2b6p: X-ray structure of lens Aquaporin-0 (AQP0) (lens MIP) in an open pore state Method: X-RAY DIFFRACTION / Resolution: 2.4 Å
Chemicals	ChemComp-MC3: 1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE / phospholipidYM ChemComp-HOH*: WATER / Water
Source	ovis aries (sheep) bos taurus (cattle)
Keywords	MEMBRANE PROTEIN / aquaporin-0 junctions / AQP0 / lens MIP / lipid-protein interactions / membrane / lipid bilayer / closed water pore / aquaporin-0; AQP0; lens MIP; open water pore; aquaporin; membrane protein;