6oly: Difference between revisions

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-'''Unreleased structure'''
-The entry 6oly is ON HOLD  until Paper Publication
+==Full-length MthK channel at 3.1 angstrom resolution==
+<StructureSection load='6oly' size='340' side='right'caption='[[6oly]], [[Resolution|resolution]] 3.11&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6oly]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OLY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OLY FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.112&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=6oly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oly OCA], [https://pdbe.org/6oly PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6oly RCSB], [https://www.ebi.ac.uk/pdbsum/6oly PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6oly ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MTHK_METTH MTHK_METTH] Calcium-gated potassium channel.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Potassium channels are presumed to have two allosterically coupled gates, the activation gate and the selectivity filter gate, that control channel opening, closing, and inactivation. However, the molecular mechanism of how these gates regulate K(+ )ion flow through the channel remains poorly understood. An activation process, occurring at the selectivity filter, has been recently proposed for several potassium channels. Here, we use X-ray crystallography and extensive molecular dynamics simulations, to study ion permeation through a potassium channel MthK, for various opening levels of both gates. We find that the channel conductance is controlled at the selectivity filter, whose conformation depends on the activation gate. The crosstalk between the gates is mediated through a collective motion of channel helices, involving hydrophobic contacts between an isoleucine and a conserved threonine in the selectivity filter. We propose a gating model of selectivity filter-activated potassium channels, including pharmacologically relevant two-pore domain (K2P) and big potassium (BK) channels.
-Authors:
+Molecular mechanism of a potassium channel gating through activation gate-selectivity filter coupling.,Kopec W, Rothberg BS, de Groot BL Nat Commun. 2019 Nov 26;10(1):5366. doi: 10.1038/s41467-019-13227-w. PMID:31772184<ref>PMID:31772184</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 6oly" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Potassium channel 3D structures|Potassium channel 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Methanothermobacter thermautotrophicus]]
+[[Category: Rothberg BS]]