View source for 5nwi


==14-3-3c in complex with CPP==
<StructureSection load='5nwi' size='340' side='right'caption='[[5nwi]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5nwi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] and [https://en.wikipedia.org/wiki/Nicotiana_tabacum Nicotiana tabacum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NWI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NWI 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]] 2.35&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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=5nwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nwi OCA], [https://pdbe.org/5nwi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nwi RCSB], [https://www.ebi.ac.uk/pdbsum/5nwi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nwi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/1433C_TOBAC 1433C_TOBAC] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Plants acquire potassium (K+) ions for cell growth and movement via regulated diffusion through K+ channels. Here, we present crystallographic and functional data showing that the K+ inward rectifier KAT1 (K+Arabidopsis thaliana 1) channel is regulated by 14-3-3 proteins and further modulated by the phytotoxin fusicoccin, in analogy to the H+-ATPase. We identified a 14-3-3 mode III binding site at the very C terminus of KAT1 and cocrystallized it with tobacco (Nicotiana tabacum) 14-3-3 proteins to describe the protein complex at atomic detail. Validation of this interaction by electrophysiology shows that 14-3-3 binding augments KAT1 conductance by increasing the maximal current and by positively shifting the voltage dependency of gating. Fusicoccin potentiates the 14-3-3 effect on KAT1 activity by stabilizing their interaction. Crystal structure of the ternary complex reveals a noncanonical binding site for the toxin that adopts a novel conformation. The structural insights underscore the adaptability of fusicoccin, predicting more potential targets than so far anticipated. The data further advocate a common mechanism of regulation of the proton pump and a potassium channel, two essential elements in K+ uptake in plant cells.

Fusicoccin Activates KAT1 Channels by Stabilizing Their Interaction with 14-3-3 Proteins.,Saponaro A, Porro A, Chaves-Sanjuan A, Nardini M, Rauh O, Thiel G, Moroni A Plant Cell. 2017 Oct;29(10):2570-2580. doi: 10.1105/tpc.17.00375. Epub 2017 Sep, 29. PMID:28970335<ref>PMID:28970335</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5nwi" style="background-color:#fffaf0;"></div>

==See Also==
*[[14-3-3 protein 3D structures|14-3-3 protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Nicotiana tabacum]]
[[Category: Chaves-Sanjuan A]]
[[Category: Moroni A]]
[[Category: Nardini M]]
[[Category: Porro A]]
[[Category: Saponaro A]]
[[Category: Thiel G]]