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[[Image:2b6o.gif|left|200px]]
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{{STRUCTURE_2b6o|  PDB=2b6o  |  SCENE=  }}
'''electron crystallographic structure of lens Aquaporin-0 (AQP0) (lens MIP) at 1.9A resolution, in a closed pore state'''


==Electron crystallographic structure of lens Aquaporin-0 (AQP0) (lens MIP) at 1.9A resolution, in a closed pore state==
<StructureSection load='2b6o' size='340' side='right'caption='[[2b6o]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2b6o]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B6O FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron crystallography, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MC3:1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE'>MC3</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2b6o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b6o OCA], [https://pdbe.org/2b6o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b6o RCSB], [https://www.ebi.ac.uk/pdbsum/2b6o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b6o ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MIP_SHEEP MIP_SHEEP] Water channel. May be responsible for regulating the osmolarity of the lens. Interactions between homotetramers from adjoining membranes may stabilize cell junctions in the eye lens core.<ref>PMID:15141214</ref> <ref>PMID:15351655</ref> <ref>PMID:20389283</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b6/2b6o_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2b6o ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:16319884</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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].
</div>
<div class="pdbe-citations 2b6o" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Aquaporin 3D structures|Aquaporin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Ovis aries]]
[[Category: Ovis aries]]
[[Category: Single protein]]
[[Category: Cheng Y]]
[[Category: Cheng, Y.]]
[[Category: Fujiyoshi Y]]
[[Category: Fujiyoshi, Y.]]
[[Category: Gonen T]]
[[Category: Gonen, T.]]
[[Category: Harrison SC]]
[[Category: Harrison, S C.]]
[[Category: Hiroaki Y]]
[[Category: Hiroaki, Y.]]
[[Category: Sliz P]]
[[Category: Sliz, P.]]
[[Category: Walz T]]
[[Category: Walz, T.]]
[[Category: Aqp0]]
[[Category: Aquaporin-0 junction]]
[[Category: Closed water pore]]
[[Category: Electron crystallography]]
[[Category: Lens mip]]
[[Category: Lipid bilayer]]
[[Category: Lipid-protein interaction]]
[[Category: Membrane]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 19:55:21 2008''

Latest revision as of 07:34, 23 August 2023

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

2b6o, resolution 1.90Å

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