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 [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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4IA4 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1z98|1z98]], [[2b5f|2b5f]], [[3cll|3cll]], [[3cn5|3cn5]], [[3cn6|3cn6]]</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ia4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ia4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ia4 RCSB], [http://www.ebi.ac.uk/pdbsum/4ia4 PDBsum]</span></td></tr> | |||
</table> | |||
<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> | |||
==See Also== | |||
*[[Aquaporin|Aquaporin]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[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: Aquaporin]] | ||
[[Category: Integral membrane protein]] | [[Category: Integral membrane protein]] | ||
[[Category: Transport protein]] | [[Category: Transport protein]] | ||
[[Category: Water channel protein]] | [[Category: Water channel protein]] | ||
Revision as of 12:12, 21 December 2014
Structure of the spinach aquaporin SoPIP2;1 at pH 6
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