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

Lejla Zubcevic, Vassiliy N. Bavro, Joao R.C. Muniz, Matthias R. Schmidt, Shizhen Wang, Rita De Zorzi, Catherine Venien-Bryan, Mark S.P. Sansom, Colin G. Nichols, Stephen J. Tucker

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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.

Original languageEnglish
Pages (from-to)143-151
Number of pages9
JournalJournal of Biological Chemistry
Volume289
Issue number1
DOIs
StatePublished - Jan 3 2014

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    Zubcevic, L., Bavro, V. N., Muniz, J. R. C., Schmidt, M. R., Wang, S., De Zorzi, R., Venien-Bryan, C., Sansom, M. S. P., Nichols, C. G., & Tucker, S. J. (2014). Control of KirBac3.1 potassium channel gating at the interface between cytoplasmic domains. Journal of Biological Chemistry, 289(1), 143-151. https://doi.org/10.1074/jbc.M113.501833