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| | <StructureSection load='5nwj' size='340' side='right'caption='[[5nwj]], [[Resolution|resolution]] 2.07Å' scene=''> | | <StructureSection load='5nwj' size='340' side='right'caption='[[5nwj]], [[Resolution|resolution]] 2.07Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5nwj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/American_tobacco American tobacco]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NWJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5NWJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5nwj]] 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=5NWJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NWJ FirstGlance]. <br> |
| - | </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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.07Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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'>[http://proteopedia.org/fgij/fg.htm?mol=5nwj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nwj OCA], [http://pdbe.org/5nwj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nwj RCSB], [http://www.ebi.ac.uk/pdbsum/5nwj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nwj ProSAT]</span></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=5nwj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nwj OCA], [https://pdbe.org/5nwj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nwj RCSB], [https://www.ebi.ac.uk/pdbsum/5nwj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nwj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/KAT1_ARATH KAT1_ARATH]] Highly selective inward-rectifying potassium channel. This voltage-gated channel could mediate long-term potassium influx into guard cells leading to stomatal opening. Assuming opened or closed conformations in response to the voltage difference across the membrane, the channel is activated by hyperpolarization. The channel activity is enhanced upon external acidification. Also permeable to ammonium ions. Blocked by tetraethylammonium and barium ions.<ref>PMID:8966547</ref> | + | [https://www.uniprot.org/uniprot/1433C_TOBAC 1433C_TOBAC] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: American tobacco]] | + | [[Category: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chaves-Sanjuan, A]] | + | [[Category: Nicotiana tabacum]] |
| - | [[Category: Moroni, A]] | + | [[Category: Chaves-Sanjuan A]] |
| - | [[Category: Nardini, M]] | + | [[Category: Moroni A]] |
| - | [[Category: Porro, A]] | + | [[Category: Nardini M]] |
| - | [[Category: Saponaro, A]] | + | [[Category: Porro A]] |
| - | [[Category: Thiel, G]] | + | [[Category: Saponaro A]] |
| - | [[Category: 14-3-3]]
| + | [[Category: Thiel G]] |
| - | [[Category: Channel]]
| + | |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Fusicoccin]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
5nwj is a 2 chain structure with sequence from Arabidopsis thaliana and Nicotiana tabacum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 2.07Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
1433C_TOBAC
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Saponaro A, Porro A, Chaves-Sanjuan A, Nardini M, Rauh O, Thiel G, Moroni A. Fusicoccin Activates KAT1 Channels by Stabilizing Their Interaction with 14-3-3 Proteins. Plant Cell. 2017 Oct;29(10):2570-2580. doi: 10.1105/tpc.17.00375. Epub 2017 Sep, 29. PMID:28970335 doi:http://dx.doi.org/10.1105/tpc.17.00375
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