2b6o
From Proteopedia
(New page: 200px<br /><applet load="2b6o" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b6o, resolution 1.90Å" /> '''electron crystallogr...) |
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| - | [[Image:2b6o.gif|left|200px]]<br /><applet load="2b6o" size=" | + | [[Image:2b6o.gif|left|200px]]<br /><applet load="2b6o" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2b6o, resolution 1.90Å" /> | caption="2b6o, resolution 1.90Å" /> | ||
'''electron crystallographic structure of lens Aquaporin-0 (AQP0) (lens MIP) at 1.9A resolution, in a closed pore state'''<br /> | '''electron crystallographic structure of lens Aquaporin-0 (AQP0) (lens MIP) at 1.9A resolution, in a closed pore state'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Lens-specific aquaporin-0 (AQP0) functions as a specific water pore and | + | 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== | ==About this Structure== | ||
| - | 2B6O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries] with MC3 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2B6O is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries] with <scene name='pdbligand=MC3:'>MC3</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B6O OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Fujiyoshi, Y.]] | [[Category: Fujiyoshi, Y.]] | ||
[[Category: Gonen, T.]] | [[Category: Gonen, T.]] | ||
| - | [[Category: Harrison, S | + | [[Category: Harrison, S C.]] |
[[Category: Hiroaki, Y.]] | [[Category: Hiroaki, Y.]] | ||
[[Category: Sliz, P.]] | [[Category: Sliz, P.]] | ||
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[[Category: membrane]] | [[Category: membrane]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:34:41 2008'' |
Revision as of 14:34, 21 February 2008
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electron crystallographic structure of lens Aquaporin-0 (AQP0) (lens MIP) at 1.9A resolution, in a closed 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
2B6O is a Single protein structure of sequence from Ovis aries with as ligand. 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 Thu Feb 21 16:34:41 2008
