4ia4
From Proteopedia
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| - | {{STRUCTURE_4ia4| PDB=4ia4 | SCENE= }} | ||
| - | ===Structure of the spinach aquaporin SoPIP2;1 at pH 6=== | ||
| - | {{ABSTRACT_PUBMED_23454640}} | ||
| - | == | + | ==Structure of the spinach aquaporin SoPIP2;1 at pH 6== |
| - | [[4ia4]] is a 4 chain structure with sequence from [ | + | <StructureSection load='4ia4' size='340' side='right'caption='[[4ia4]], [[Resolution|resolution]] 3.10Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4ia4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Spinacia_oleracea Spinacia oleracea]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4IA4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4IA4 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</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=4ia4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ia4 OCA], [https://pdbe.org/4ia4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ia4 RCSB], [https://www.ebi.ac.uk/pdbsum/4ia4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ia4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q41372_SPIOL Q41372_SPIOL] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Plants have evolved to cope with fluctuations in water supply by gating their water channels known as aquaporins. During flooding, a rapid drop of cytosolic pH due to anoxia leads to a simultaneous closure of the aquaporins in the plasma membrane. The closing mechanism has been suggested to involve a conserved histidine on cytosolic loop D. Here we report the crystal structure of a spinach aquaporin at low pH, revealing for the first time the structural basis for how this pH-sensitive histidine helps to keep the aquaporin in a closed state. | ||
| - | + | Structural basis for pH gating of plant aquaporins.,Frick A, Jarva M, Tornroth-Horsefield S FEBS Lett. 2013 Apr 2;587(7):989-93. doi: 10.1016/j.febslet.2013.02.038. Epub, 2013 Feb 27. PMID:23454640<ref>PMID:23454640</ref> | |
| - | <ref | + | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4ia4" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Aquaporin 3D structures|Aquaporin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Spinacia oleracea]] | [[Category: Spinacia oleracea]] | ||
| - | [[Category: Frick | + | [[Category: Frick A]] |
| - | [[Category: Jarva | + | [[Category: Jarva M]] |
| - | [[Category: Tornroth-Horsefield | + | [[Category: Tornroth-Horsefield S]] |
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Current revision
Structure of the spinach aquaporin SoPIP2;1 at pH 6
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