3m9i
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:3m9i.jpg|left|200px]] | ||
| - | < | + | ==Electron crystallographic structure of lens Aquaporin-0 (AQP0) (lens MIP) in E. coli polar lipids== |
| - | + | <StructureSection load='3m9i' size='340' side='right'caption='[[3m9i]], [[Resolution|resolution]] 2.50Å' scene=''> | |
| - | You may | + | == Structural highlights == |
| - | + | <table><tr><td colspan='2'>[[3m9i]] 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=3M9I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M9I 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]] 2.5Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3PE:1,2-DIACYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE'>3PE</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=3m9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m9i OCA], [https://pdbe.org/3m9i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m9i RCSB], [https://www.ebi.ac.uk/pdbsum/3m9i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m9i 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/m9/3m9i_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=3m9i ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | We have previously described the interactions of aquaporin-0 (AQP0) with dimyristoyl phosphatidylcholine (DMPC) lipids. We have now determined the 2.5 A structure of AQP0 in two-dimensional (2D) crystals formed with Escherichia coli polar lipids (EPLs), which differ from DMPC both in headgroups and acyl chains. Comparison of the two structures shows that AQP0 does not adapt to the different length of the acyl chains in EPLs and that the distance between the phosphodiester groups in the two leaflets of the DMPC and EPL bilayers is almost identical. The EPL headgroups interact differently with AQP0 than do those of DMPC, but the acyl chains in the EPL and DMPC bilayers occupy similar positions. The interactions of annular lipids with membrane proteins seem to be driven by the propensity of the acyl chains to fill gaps in the protein surface. Interactions of the lipid headgroups may be responsible for the specific interactions found in tightly bound lipids but seem to have a negligible effect on interactions of generic annular lipids with membrane proteins. | ||
| - | + | Principles of membrane protein interactions with annular lipids deduced from aquaporin-0 2D crystals.,Hite RK, Li Z, Walz T EMBO J. 2010 May 19;29(10):1652-8. Epub 2010 Apr 13. PMID:20389283<ref>PMID:20389283</ref> | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 3m9i" style="background-color:#fffaf0;"></div> | ||
| - | + | ==See Also== | |
| - | + | *[[Aquaporin 3D structures|Aquaporin 3D structures]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | [[Category: Large Structures]] |
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[[Category: Ovis aries]] | [[Category: Ovis aries]] | ||
| - | [[Category: Hite | + | [[Category: Hite RK]] |
| - | [[Category: Li | + | [[Category: Li Z]] |
| - | [[Category: Walz | + | [[Category: Walz T]] |
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Current revision
Electron crystallographic structure of lens Aquaporin-0 (AQP0) (lens MIP) in E. coli polar lipids
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Categories: Large Structures | Ovis aries | Hite RK | Li Z | Walz T
