7wsw

From Proteopedia

(Difference between revisions)

Current revision

Cryo-EM structure of the Potassium channel AKT1 from Arabidopsis thaliana

Structural highlights

7wsw is a 4 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.4Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AKT1_ARATH Highly selective inward-rectifying potassium channel that mediate potassium uptake by plant roots in response to low K(+) conditions, by a calcium-, CBL-, and CIPK-dependent pathway. Positively regulated by phosphorylation by CIPK23. Negatively regulated by a kinase-independent regulatory mechanism involving a competing direct binding of CBL10. Involved in the stomatal regulation by monitoring the turgor pressure in guard cells. Assuming opened or closed conformations in response to the voltage difference across the membrane, the channel is activated by hyperpolarization. May interact with the cytoskeleton or with regulatory proteins.^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

The voltage-gated potassium channel AKT1 is responsible for primary K(+) uptake in Arabidopsis roots. AKT1 is functionally activated through phosphorylation and negatively regulated by a potassium channel alpha-subunit AtKC1. However, the molecular basis for the modulation mechanism remains unclear. Here we report the structures of AKT1, phosphorylated-AKT1, a constitutively-active variant, and AKT1-AtKC1 complex. AKT1 is assembled in 2-fold symmetry at the cytoplasmic domain. Such organization appears to sterically hinder the reorientation of C-linkers during ion permeation. Phosphorylated-AKT1 adopts an alternate 4-fold symmetric conformation at cytoplasmic domain, which indicates conformational changes associated with symmetry switch during channel activation. To corroborate this finding, we perform structure-guided mutagenesis to disrupt the dimeric interface and identify a constitutively-active variant Asp379Ala mediates K(+) permeation independently of phosphorylation. This variant predominantly adopts a 4-fold symmetric conformation. Furthermore, the AKT1-AtKC1 complex assembles in 2-fold symmetry. Together, our work reveals structural insight into the regulatory mechanism for AKT1.

Structural basis for the activity regulation of a potassium channel AKT1 from Arabidopsis.,Lu Y, Yu M, Jia Y, Yang F, Zhang Y, Xu X, Li X, Yang F, Lei J, Wang Y, Yang G Nat Commun. 2022 Sep 27;13(1):5682. doi: 10.1038/s41467-022-33420-8. PMID:36167696^[6]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Pilot G, Gaymard F, Mouline K, Cherel I, Sentenac H. Regulated expression of Arabidopsis shaker K+ channel genes involved in K+ uptake and distribution in the plant. Plant Mol Biol. 2003 Mar;51(5):773-87. PMID:12678562
↑ Xu J, Li HD, Chen LQ, Wang Y, Liu LL, He L, Wu WH. A protein kinase, interacting with two calcineurin B-like proteins, regulates K+ transporter AKT1 in Arabidopsis. Cell. 2006 Jun 30;125(7):1347-60. PMID:16814720 doi:http://dx.doi.org/S0092-8674(06)00769-0
↑ Li L, Kim BG, Cheong YH, Pandey GK, Luan S. A Ca(2)+ signaling pathway regulates a K(+) channel for low-K response in Arabidopsis. Proc Natl Acad Sci U S A. 2006 Aug 15;103(33):12625-30. Epub 2006 Aug 8. PMID:16895985 doi:http://dx.doi.org/0605129103
↑ Lee SC, Lan WZ, Kim BG, Li L, Cheong YH, Pandey GK, Lu G, Buchanan BB, Luan S. A protein phosphorylation/dephosphorylation network regulates a plant potassium channel. Proc Natl Acad Sci U S A. 2007 Oct 2;104(40):15959-64. Epub 2007 Sep 26. PMID:17898163 doi:http://dx.doi.org/0707912104
↑ Hirsch RE, Lewis BD, Spalding EP, Sussman MR. A role for the AKT1 potassium channel in plant nutrition. Science. 1998 May 8;280(5365):918-21. PMID:9572739
↑ Lu Y, Yu M, Jia Y, Yang F, Zhang Y, Xu X, Li X, Yang F, Lei J, Wang Y, Yang G. Structural basis for the activity regulation of a potassium channel AKT1 from Arabidopsis. Nat Commun. 2022 Sep 27;13(1):5682. doi: 10.1038/s41467-022-33420-8. PMID:36167696 doi:http://dx.doi.org/10.1038/s41467-022-33420-8

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7wsw"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[7wsw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WSW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WSW FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PTY:PHOSPHATIDYLETHANOLAMINE'>PTY</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PTY:PHOSPHATIDYLETHANOLAMINE'>PTY</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=7wsw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wsw OCA], [https://pdbe.org/7wsw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wsw RCSB], [https://www.ebi.ac.uk/pdbsum/7wsw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wsw ProSAT]</span></td></tr>
 </table>
@@ Line 18: / Line 19: @@
 </div>
 <div class="pdbe-citations 7wsw" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Potassium channel 3D structures|Potassium channel 3D structures]]
 == References ==
 <references/>

7wsw

From Proteopedia

Current revision

Cryo-EM structure of the Potassium channel AKT1 from Arabidopsis thaliana

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox