期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 289, 期 1, 页码 143-151出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M113.501833
关键词
Crystal Structure; Ion Channels; Membrane Proteins; Molecular Dynamics; Potassium Channels; Channel Gating; Kir Channel; KirBac
资金
- National Institute of Health [HL54171]
- Biotechnology and Biological Sciences Research Council
- Wellcome Trust
- BBSRC [BB/F013035/1, BB/H000267/1, BB/L002558/1, BB/I019855/1] Funding Source: UKRI
- EPSRC [EP/J010421/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BEP17032, BB/H000267/1, BB/I019855/1, B19456, BB/L002558/1, BB/F013035/1, BBS/B/16011] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [EP/J010421/1] Funding Source: researchfish
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.
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