Helical jackknives control the gates of the double-pore K+ uptake system KtrAB
DC Element | Wert | Sprache |
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dc.contributor.author | Diskowski, Marina | |
dc.contributor.author | Mehdipour, Ahmad Reza | |
dc.contributor.author | Wunnicke, Dorith | |
dc.contributor.author | Mills, Deryck J. | |
dc.contributor.author | Mikusevic, Vedrana | |
dc.contributor.author | Baerland, Natalie | |
dc.contributor.author | Hoffmann, Jan | |
dc.contributor.author | Morgner, Nina | |
dc.contributor.author | Steinhoff, Heinz-Juergen | |
dc.contributor.author | Hummer, Gerhard | |
dc.contributor.author | Vonck, Janet | |
dc.contributor.author | Haenelt, Inga | |
dc.date.accessioned | 2021-12-23T16:16:52Z | - |
dc.date.available | 2021-12-23T16:16:52Z | - |
dc.date.issued | 2017 | |
dc.identifier.issn | 2050084X | |
dc.identifier.uri | https://osnascholar.ub.uni-osnabrueck.de/handle/unios/12086 | - |
dc.description.abstract | Ion channel gating is essential for cellular homeostasis and is tightly controlled. In some eukaryotic and most bacterial ligand-gated K+ channels, RCK domains regulate ion fluxes. Until now, a single regulatory mechanism has been proposed for all RCK-regulated channels, involving signal transduction from the RCK domain to the gating area. Here, we present an inactive ADP-bound structure of KtrAB from Vibrio alginolyticus, determined by cryo-electron microscopy, which, combined with EPR spectroscopy and molecular dynamics simulations, uncovers a novel regulatory mechanism for ligand-induced action at a distance. Exchange of activating ATP to inactivating ADP triggers short helical segments in the K+-translocating KtrB dimer to organize into two long helices that penetrate deeply into the regulatory RCK domains, thus connecting nucleotide-binding sites and ion gates. As KtrAB and its homolog TrkAH have been implicated as bacterial pathogenicity factors, the discovery of this functionally relevant inactive conformation may advance structure-guided drug development. | |
dc.description.sponsorship | Deutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [HA 6322/3-1, HA 6322/2-1, SFB 807]; Max-Planck-GesellschaftMax Planck Society; Deutsche Forschungsgemeinschaft HA 6322/3-1 Inga Hanelt; Max-Planck-Gesellschaft Ahmad Reza Mehdipour Deryck J Mills Gerhard Hummer Janet Vonck; Deutsche Forschungsgemeinschaft HA 6322/2-1 Inga Hanelt; Deutsche Forschungsgemeinschaft SFB 807 Nina Morgner Gerhard Hummer Inga Hanelt; Deutsche Forschungsgemeinschaft CEF Macromolecular Complexes Ahmad Reza Mehdipour Inga Hanelt | |
dc.language.iso | en | |
dc.publisher | ELIFE SCIENCES PUBLICATIONS LTD | |
dc.relation.ispartof | ELIFE | |
dc.subject | BETAINE CARRIER BETP | |
dc.subject | Biology | |
dc.subject | CORYNEBACTERIUM-GLUTAMICUM | |
dc.subject | CRYSTAL-STRUCTURE | |
dc.subject | ESCHERICHIA-COLI | |
dc.subject | ION-CHANNEL | |
dc.subject | Life Sciences & Biomedicine - Other Topics | |
dc.subject | MEMBRANE REGION M-2C2 | |
dc.subject | MOLECULAR-DYNAMICS | |
dc.subject | POTASSIUM-TRANSPORT | |
dc.subject | SEQUENCE ALIGNMENT | |
dc.subject | VIBRIO-ALGINOLYTICUS | |
dc.title | Helical jackknives control the gates of the double-pore K+ uptake system KtrAB | |
dc.type | journal article | |
dc.identifier.doi | 10.7554/eLife.24303 | |
dc.identifier.isi | ISI:000402308200001 | |
dc.description.volume | 6 | |
dc.contributor.orcid | 0000-0002-1872-490X | |
dc.contributor.orcid | 0000-0002-5888-0157 | |
dc.contributor.orcid | 0000-0003-1495-3163 | |
dc.contributor.orcid | 0000-0001-7768-746X | |
dc.contributor.orcid | 0000-0002-0193-3334 | |
dc.contributor.orcid | 0000-0001-5659-8863 | |
dc.contributor.orcid | 0000-0002-9666-9571 | |
dc.contributor.researcherid | AAY-5243-2021 | |
dc.contributor.researcherid | O-7021-2018 | |
dc.contributor.researcherid | H-3791-2014 | |
dc.contributor.researcherid | N-2982-2016 | |
dc.contributor.researcherid | A-2546-2013 | |
dc.publisher.place | SHERATON HOUSE, CASTLE PARK, CAMBRIDGE, CB3 0AX, ENGLAND | |
dcterms.isPartOf.abbreviation | eLife | |
dcterms.oaStatus | Green Published, gold | |
crisitem.author.dept | FB 04 - Physik | - |
crisitem.author.deptid | fb04 | - |
crisitem.author.parentorg | Universität Osnabrück | - |
crisitem.author.netid | StHe633 | - |
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geprüft am 06.06.2024