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Control of KirBac3.1 Potassium Channel Gating at the Interface between Cytoplasmic Domains

DOI: 10.1074/jbc.M113.501833 DOI Help
PMID: 24257749 PMID Help

Authors: L. Zubcevic (University of Oxford) , V. N. Bavro (University of Oxford) , J. R. C Muniz (University of Oxford) , M. R. Schmidt (University of Oxford) , S. Wang (Washington University) , R. De Zorzi (Harvard Medical School) , C. Venien-bryan (Harvard Medical School) , M. S. P. Sansom (University of Oxford) , C. G. Nichols (Washington University) , S. J. Tucker (University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Biological Chemistry , VOL 289 (1) , PAGES 143 - 151

State: Published (Approved)
Published: January 2014

Open Access Open Access

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.

Journal Keywords: Bacterial; Ion; Magnetospirillum; Mutation; Missense; Potassium; Inwardly; Protein; Tertiary

Subject Areas: Biology and Bio-materials


Instruments: I24-Microfocus Macromolecular Crystallography

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