4ia4: Difference between revisions
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==Structure of the spinach aquaporin SoPIP2;1 at pH 6== | |||
<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> | |||
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: Frick A]] | |||
[[Category: Jarva M]] | |||
[[Category: Tornroth-Horsefield S]] | |||
Latest revision as of 14:13, 8 November 2023
Structure of the spinach aquaporin SoPIP2;1 at pH 6
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