2b6o

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[[Image:2b6o.gif|left|200px]]<br /><applet load="2b6o" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2b6o.gif|left|200px]]
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caption="2b6o, resolution 1.90&Aring;" />
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'''electron crystallographic structure of lens Aquaporin-0 (AQP0) (lens MIP) at 1.9A resolution, in a closed pore state'''<br />
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{{Structure
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|PDB= 2b6o |SIZE=350|CAPTION= <scene name='initialview01'>2b6o</scene>, resolution 1.90&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MC3:1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE'>MC3</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''electron crystallographic structure of lens Aquaporin-0 (AQP0) (lens MIP) at 1.9A resolution, in a closed pore state'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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2B6O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B6O OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16319884 16319884]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16319884 16319884]
[[Category: Ovis aries]]
[[Category: Ovis aries]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: MC3]]
[[Category: MC3]]
[[Category: aqp0]]
[[Category: aqp0]]
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[[Category: aquaporin-0 junctions]]
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[[Category: aquaporin-0 junction]]
[[Category: closed water pore]]
[[Category: closed water pore]]
[[Category: electron crystallography]]
[[Category: electron crystallography]]
[[Category: lens mip]]
[[Category: lens mip]]
[[Category: lipid bilayer]]
[[Category: lipid bilayer]]
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[[Category: lipid-protein interactions]]
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[[Category: lipid-protein interaction]]
[[Category: membrane]]
[[Category: membrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:34:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:58:12 2008''

Revision as of 13:58, 20 March 2008


PDB ID 2b6o

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, resolution 1.90Å
Ligands:
Coordinates: save as pdb, mmCIF, xml



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. 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

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