7xuf: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7xuf]] 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=7XUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XUF FirstGlance]. <br> | <table><tr><td colspan='2'>[[7xuf]] 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=7XUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XUF 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></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]] 3.3Å</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></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=7xuf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xuf OCA], [https://pdbe.org/7xuf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xuf RCSB], [https://www.ebi.ac.uk/pdbsum/7xuf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xuf 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=7xuf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xuf OCA], [https://pdbe.org/7xuf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xuf RCSB], [https://www.ebi.ac.uk/pdbsum/7xuf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xuf ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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</div> | </div> | ||
<div class="pdbe-citations 7xuf" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 7xuf" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Potassium channel 3D structures|Potassium channel 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 10:29, 3 July 2024
Cryo-EM structure of the AKT1-AtKC1 complex from Arabidopsis thalianaCryo-EM structure of the AKT1-AtKC1 complex from Arabidopsis thaliana
Structural highlights
FunctionKAT3_ARATH Probable modulatory (alpha) subunit of inward-rectifying potassium channels. Could mediate potassium uptake from the soil solution by plant roots in association with AKT1.[1] [2] Publication Abstract from PubMedThe 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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