4ia4: Difference between revisions

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{{STRUCTURE_4ia4|  PDB=4ia4  |  SCENE=  }}
===Structure of the spinach aquaporin SoPIP2;1 at pH 6===
{{ABSTRACT_PUBMED_23454640}}


==About this Structure==
==Structure of the spinach aquaporin SoPIP2;1 at pH 6==
[[4ia4]] is a 4 chain structure with sequence from [http://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].  
<StructureSection load='4ia4' size='340' side='right'caption='[[4ia4]], [[Resolution|resolution]] 3.10&Aring;' 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]] 3.1&#8491;</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.


==Reference==
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 group="xtra">PMID:023454640</ref><references group="xtra"/><references/>
 
From MEDLINE&reg;/PubMed&reg;, 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, A.]]
[[Category: Frick A]]
[[Category: Jarva, M.]]
[[Category: Jarva M]]
[[Category: Tornroth-Horsefield, S.]]
[[Category: Tornroth-Horsefield S]]
[[Category: Aquaporin]]
[[Category: Integral membrane protein]]
[[Category: Transport protein]]
[[Category: Water channel protein]]
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