dc.publisher: Nature Publishing Group access_endpoint: https://www.nature.com/platform/readcube-access og:image: https://media.springernature.com/m685/springer-static/image/art%3A10.1038%2Fs41467-019-13227-w/MediaObjects/41467_2019_13227_Fig1_HTML.png WT.cg_s: Article twitter:card: summary og:site_name: Nature Communications citation_reference: Hille, B. Ion Channels of Excitable Membranes. 3rd edn, 11 (Sinauer, Sunderland, 2001). citation_journal_title: Nature Communications dc.rights: ©2019 Macmillan Publishers Limited. All Rights Reserved. og:description: Potassium channels such as MthK are presumed to have two allosterically coupled gates, the activation gate and the selectivity filter gate, that control gating transitions. Here authors use X-ray crystallography and molecular dynamics simulations on MthK and observe crosstalk between the gates. prism.issn: 2041-1723 WT.cg_n: Nature Communications prism.number: 1 citation_issn: 2041-1723 twitter:image:alt: Content cover image WT.z_subject_term_id: biophysics;computational-biophysics;ion-channels;potassium-channels;structural-biology dc:title: Molecular mechanism of a potassium channel gating through activation gate-selectivity filter coupling | Nature Communications citation_language: en Content-Encoding: UTF-8 WT.z_cg_type: Nature Research Journals citation_pdf_url: https://www.nature.com/articles/s41467-019-13227-w.pdf robots: noarchive WT.z_primary_atype: Research citation_lastpage: 15 DOI: 10.1038/s41467-019-13227-w application-name: Nature citation_fulltext_world_readable: citation_journal_abbrev: Nat Commun prism.rightsAgent: journalpermissions@springernature.com citation_author: Wojciech Kopec dc.date: 2019-11-26 WT.z_subject_term: Biophysics;Computational biophysics;Ion channels;Potassium channels;Structural biology WT.z_bandiera_abtest: a citation_issue: 1 prism.volume: 10 WT.template: oscar prism.publicationName: Nature Communications citation_doi: 10.1038/s41467-019-13227-w dc.title: Molecular mechanism of a potassium channel gating through activation gate-selectivity filter coupling prism.url: https://www.nature.com/articles/s41467-019-13227-w citation_volume: 10 dc.language: En Content-Language: en msapplication-config: /static/browserconfig.e35b3b052c.xml theme-color: #000000 prism.endingPage: 15 citation_title: Molecular mechanism of a potassium channel gating through activation gate-selectivity filter coupling citation_author_institution: Biomolecular Dynamics Group, Max Planck Institute for Biophysical Chemistry, Göttingen, Germany access: Yes citation_publisher: Nature Publishing Group dc.format: text/html description: 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. Potassium channels such as MthK are presumed to have two allosterically coupled gates, the activation gate and the selectivity filter gate, that control gating transitions. Here authors use X-ray crystallography and molecular dynamics simulations on MthK and observe crosstalk between the gates. title: Molecular mechanism of a potassium channel gating through activation gate-selectivity filter coupling | Nature Communications twitter:image: https://media.springernature.com/full/springer-static/image/art%3A10.1038%2Fs41467-019-13227-w/MediaObjects/41467_2019_13227_Fig1_HTML.png citation_online_date: 2019/11/26 twitter:site: @NatureComms dc.source: Nature Communications 2019 10:1 dc.type: OriginalPaper dc.copyright: 2019 The Author(s) dc.creator: Wojciech Kopec citation_fulltext_html_url: https://www.nature.com/articles/s41467-019-13227-w WT.page_categorisation: Article_HTML prism.publicationDate: 2019-11-26 Content-Type: text/html; charset=UTF-8 journal_id: 41467 X-Parsed-By: org.apache.tika.parser.DefaultParser dc.description: 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. Potassium channels such as MthK are presumed to have two allosterically coupled gates, the activation gate and the selectivity filter gate, that control gating transitions. Here authors use X-ray crystallography and molecular dynamics simulations on MthK and observe crosstalk between the gates. twitter:title: Molecular mechanism of a potassium channel gating through activation g og:type: article citation_article_type: Article og:title: Molecular mechanism of a potassium channel gating through activation gate-selectivity filter coupling prism.doi: doi:10.1038/s41467-019-13227-w msapplication-TileColor: #000000 X-UA-Compatible: IE=edge citation_firstpage: 1 WT.z_cc_license_type: cc_by prism.startingPage: 1 viewport: width=device-width,initial-scale=1.0,maximum-scale=2.5,user-scalable=yes twitter:description: Potassium channels such as MthK are presumed to have two allosterically coupled gates, the activation gate and the selectivity filter gate, that control gating transitions. Here authors use X-ray crystallography and molecular dynamics simulations on MthK and observe crosstalk between the gates. dc.rightsAgent: journalpermissions@springernature.com prism.section: OriginalPaper dc.identifier: doi:10.1038/s41467-019-13227-w dc.subject: Biophysics og:url: https://www.nature.com/articles/s41467-019-13227-w prism.copyright: 2019 The Author(s)