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Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains.

Zubcevic, Lejla and Bavro, Vassiliy N and Muniz, Joao RC and Schmidt, Matthias R and Wang, Shizhen and De Zorzi, Rita and Venien-Bryan, Catherine and Sansom, Mark SP and Nichols, Colin G and Tucker, Stephen J (2014) 'Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains.' The Journal of Biological Chemistry, 289 (1). 143 - 151. ISSN 0021-9258

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Abstract

KirBac channels are prokaryotic homologs of mammalian inwardly rectifying potassium (Kir) channels, and recent structures of KirBac3.1 have provided important insights into the structural basis of gating in Kir channels. In this study, we demonstrate that KirBac3.1 channel activity is strongly pH-dependent, and we used x-ray crystallography to determine the structural changes that arise from an activatory mutation (S205L) located in the cytoplasmic domain (CTD). This mutation stabilizes a novel energetically favorable open conformation in which changes at the intersubunit interface in the CTD also alter the electrostatic potential of the inner cytoplasmic cavity. These results provide a structural explanation for the activatory effect of this mutation and provide a greater insight into the role of the CTD in Kir channel gating.

Item Type: Article
Uncontrolled Keywords: Magnetospirillum, Bacterial Proteins, Potassium Channels, Inwardly Rectifying, Amino Acid Substitution, Ion Channel Gating, Protein Structure, Tertiary, Mutation, Missense
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculty of Science and Health > Life Sciences, School of
Depositing User: Jim Jamieson
Date Deposited: 15 Dec 2016 14:13
Last Modified: 28 Jun 2021 13:15
URI: http://repository.essex.ac.uk/id/eprint/17731

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