4chv: Difference between revisions
New page: '''Unreleased structure''' The entry 4chv is ON HOLD Authors: Kowal, J., Chami, M., Baumgartner, P., Arheit, M., Chiu, P.L., Rangl, M., Scheuring, S., Schroeder, G.F., Nimigean, C.M., S... |
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The | ==The electron crystallography structure of the cAMP-bound potassium channel MloK1== | ||
<StructureSection load='4chv' size='340' side='right'caption='[[4chv]], [[Resolution|resolution]] 7.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4chv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mesorhizobium_loti Mesorhizobium loti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CHV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CHV FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron crystallography, [[Resolution|Resolution]] 7Å</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=4chv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4chv OCA], [https://pdbe.org/4chv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4chv RCSB], [https://www.ebi.ac.uk/pdbsum/4chv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4chv ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CNGK1_RHILO CNGK1_RHILO] Cyclic nucleotide-regulated potassium channel activated by cAMP.<ref>PMID:15550244</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Cyclic nucleotide-modulated ion channels are important for signal transduction and pacemaking in eukaryotes. The molecular determinants of ligand gating in these channels are still unknown, mainly because of a lack of direct structural information. Here we report ligand-induced conformational changes in full-length MloK1, a cyclic nucleotide-modulated potassium channel from the bacterium Mesorhizobium loti, analysed by electron crystallography and atomic force microscopy. Upon cAMP binding, the cyclic nucleotide-binding domains move vertically towards the membrane, and directly contact the S1-S4 voltage sensor domains. This is accompanied by a significant shift and tilt of the voltage sensor domain helices. In both states, the inner pore-lining helices are in an 'open' conformation. We propose a mechanism in which ligand binding can favour pore opening via a direct interaction between the cyclic nucleotide-binding domains and voltage sensors. This offers a simple mechanistic hypothesis for the coupling between ligand gating and voltage sensing in eukaryotic HCN channels. | |||
Ligand-induced structural changes in the cyclic nucleotide-modulated potassium channel MloK1.,Kowal J, Chami M, Baumgartner P, Arheit M, Chiu PL, Rangl M, Scheuring S, Schroder GF, Nimigean CM, Stahlberg H Nat Commun. 2014 Jan 28;5:3106. doi: 10.1038/ncomms4106. PMID:24469021<ref>PMID:24469021</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4chv" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ion channels 3D structures|Ion channels 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mesorhizobium loti]] | |||
[[Category: Arheit M]] | |||
[[Category: Baumgartner P]] | |||
[[Category: Chami M]] | |||
[[Category: Chiu PL]] | |||
[[Category: Kowal J]] | |||
[[Category: Nimigean CM]] | |||
[[Category: Rangl M]] | |||
[[Category: Scheuring S]] | |||
[[Category: Schroeder GF]] | |||
[[Category: Stahlberg H]] | |||
Latest revision as of 14:12, 9 May 2024
The electron crystallography structure of the cAMP-bound potassium channel MloK1The electron crystallography structure of the cAMP-bound potassium channel MloK1
Structural highlights
FunctionCNGK1_RHILO Cyclic nucleotide-regulated potassium channel activated by cAMP.[1] Publication Abstract from PubMedCyclic nucleotide-modulated ion channels are important for signal transduction and pacemaking in eukaryotes. The molecular determinants of ligand gating in these channels are still unknown, mainly because of a lack of direct structural information. Here we report ligand-induced conformational changes in full-length MloK1, a cyclic nucleotide-modulated potassium channel from the bacterium Mesorhizobium loti, analysed by electron crystallography and atomic force microscopy. Upon cAMP binding, the cyclic nucleotide-binding domains move vertically towards the membrane, and directly contact the S1-S4 voltage sensor domains. This is accompanied by a significant shift and tilt of the voltage sensor domain helices. In both states, the inner pore-lining helices are in an 'open' conformation. We propose a mechanism in which ligand binding can favour pore opening via a direct interaction between the cyclic nucleotide-binding domains and voltage sensors. This offers a simple mechanistic hypothesis for the coupling between ligand gating and voltage sensing in eukaryotic HCN channels. Ligand-induced structural changes in the cyclic nucleotide-modulated potassium channel MloK1.,Kowal J, Chami M, Baumgartner P, Arheit M, Chiu PL, Rangl M, Scheuring S, Schroder GF, Nimigean CM, Stahlberg H Nat Commun. 2014 Jan 28;5:3106. doi: 10.1038/ncomms4106. PMID:24469021[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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