Titre
High-Resolution Cryoelectron Microscopy Structure of the Cyclic Nucleotide-Modulated Potassium Channel MloK1 in a Lipid Bilayer.
Type
article
Institution
Externe
Périodique
Auteur(s)
Kowal, J.
Auteure/Auteur
Biyani, N.
Auteure/Auteur
Chami, M.
Auteure/Auteur
Scherer, S.
Auteure/Auteur
Rzepiela, A.J.
Auteure/Auteur
Baumgartner, P.
Auteure/Auteur
Upadhyay, V.
Auteure/Auteur
Nimigean, C.M.
Auteure/Auteur
Stahlberg, H.
Auteure/Auteur
Liens vers les personnes
ISSN
1878-4186
Statut éditorial
Publié
Date de publication
2018-01-02
Volume
26
Numéro
1
Première page
20
Dernière page/numéro d’article
27.e3
Peer-reviewed
Oui
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Publication Status: ppublish
Résumé
Eukaryotic cyclic nucleotide-modulated channels perform their diverse physiological roles by opening and closing their pores to ions in response to cyclic nucleotide binding. We here present a structural model for the cyclic nucleotide-modulated potassium channel homolog from Mesorhizobium loti, MloK1, determined from 2D crystals in the presence of lipids. Even though crystals diffract electrons to only ∼10 Å, using cryoelectron microscopy (cryo-EM) and recently developed computational methods, we have determined a 3D map of full-length MloK1 in the presence of cyclic AMP (cAMP) at ∼4.5 Å isotropic 3D resolution. The structure provides a clear picture of the arrangement of the cyclic nucleotide-binding domains with respect to both the pore and the putative voltage sensor domains when cAMP is bound, and reveals a potential gating mechanism in the context of the lipid-embedded channel.
Sujets
PID Serval
serval:BIB_B5652DE74C88
PMID
Open Access
Oui
Date de création
2023-06-09T14:02:36.070Z
Date de création dans IRIS
2025-05-21T01:17:26Z