6ebk: Difference between revisions
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The | ==The voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscs== | ||
<StructureSection load='6ebk' size='340' side='right' caption='[[6ebk]], [[Resolution|resolution]] 3.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ebk]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EBK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EBK FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ebk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ebk OCA], [http://pdbe.org/6ebk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ebk RCSB], [http://www.ebi.ac.uk/pdbsum/6ebk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ebk ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/KCAB2_RAT KCAB2_RAT]] Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. [[http://www.uniprot.org/uniprot/KCNA2_RAT KCNA2_RAT]] Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.<ref>PMID:7544443</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Voltage-activated potassium (Kv) channels open to conduct K(+) ions in response to membrane depolarization, and subsequently enter non-conducting states through distinct mechanisms of inactivation. X-ray structures of detergent-solubilized Kv channels appear to have captured an open state even though a non-conducting C-type inactivated state would predominate in membranes in the absence of a transmembrane voltage. However, structures for a voltage-activated ion channel in a lipid bilayer environment have not yet been reported. Here we report the structure of the Kv1.2-2.1 paddle chimera channel reconstituted into lipid nanodiscs using single-particle cryo-electron microscopy. At a resolution of ~3 A for the cytosolic domain and ~4 A for the transmembrane domain, the structure determined in nanodiscs is similar to the previously determined X-ray structure. Our findings show that large differences in structure between detergent and lipid bilayer environments are unlikely, and enable us to propose possible structural mechanisms for C-type inactivation. | |||
Single-particle cryo-EM structure of a voltage-activated potassium channel in lipid nanodiscs.,Matthies D, Bae C, Toombes GE, Fox T, Bartesaghi A, Subramaniam S, Swartz KJ Elife. 2018 Aug 15;7. pii: 37558. doi: 10.7554/eLife.37558. PMID:30109985<ref>PMID:30109985</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6ebk" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bae, C]] | [[Category: Bae, C]] | ||
[[Category: Bartesaghi, A]] | |||
[[Category: Fox, T]] | [[Category: Fox, T]] | ||
[[Category: | [[Category: Matthies, D]] | ||
[[Category: Subramaniam, S]] | |||
[[Category: Swartz, K J]] | |||
[[Category: Lipid nanodisc]] | |||
[[Category: Membrane protein]] | |||
[[Category: Potassium channel]] | |||
[[Category: Transport protein]] | |||
Revision as of 09:09, 22 August 2018
The voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscsThe voltage-activated Kv1.2-2.1 paddle chimera channel in lipid nanodiscs
Structural highlights
Function[KCAB2_RAT] Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. [KCNA2_RAT] Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.[1] Publication Abstract from PubMedVoltage-activated potassium (Kv) channels open to conduct K(+) ions in response to membrane depolarization, and subsequently enter non-conducting states through distinct mechanisms of inactivation. X-ray structures of detergent-solubilized Kv channels appear to have captured an open state even though a non-conducting C-type inactivated state would predominate in membranes in the absence of a transmembrane voltage. However, structures for a voltage-activated ion channel in a lipid bilayer environment have not yet been reported. Here we report the structure of the Kv1.2-2.1 paddle chimera channel reconstituted into lipid nanodiscs using single-particle cryo-electron microscopy. At a resolution of ~3 A for the cytosolic domain and ~4 A for the transmembrane domain, the structure determined in nanodiscs is similar to the previously determined X-ray structure. Our findings show that large differences in structure between detergent and lipid bilayer environments are unlikely, and enable us to propose possible structural mechanisms for C-type inactivation. Single-particle cryo-EM structure of a voltage-activated potassium channel in lipid nanodiscs.,Matthies D, Bae C, Toombes GE, Fox T, Bartesaghi A, Subramaniam S, Swartz KJ Elife. 2018 Aug 15;7. pii: 37558. doi: 10.7554/eLife.37558. PMID:30109985[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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