7xuf: Difference between revisions

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-'''Unreleased structure'''
-The entry 7xuf is ON HOLD  until Paper Publication
+==Cryo-EM structure of the AKT1-AtKC1 complex from Arabidopsis thaliana==
+<StructureSection load='7xuf' size='340' side='right'caption='[[7xuf]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
+== 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>
+</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>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/KAT3_ARATH KAT3_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.<ref>PMID:11904452</ref> <ref>PMID:12678562</ref>
+<div style="background-color:#fffaf0;">
+== 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.
-Authors:
+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<ref>PMID:36167696</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 7xuf" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Arabidopsis thaliana]]
+[[Category: Large Structures]]
+[[Category: Jia YT]]
+[[Category: Lei JL]]
+[[Category: Li XM]]
+[[Category: Lu YM]]
+[[Category: Xu X]]
+[[Category: Yang F]]
+[[Category: Yang GH]]
+[[Category: Zhang YM]]