Crystal Structure of the Potassium Channel KirBac1.1 in the Closed State

Author:

Kuo Anling1234,Gulbis Jacqueline M.1234,Antcliff Jennifer F.1234,Rahman Tahmina1234,Lowe Edward D.1234,Zimmer Jochen1234,Cuthbertson Jonathan1234,Ashcroft Frances M.1234,Ezaki Takayuki1234,Doyle Declan A.1234

Affiliation:

1. University of Oxford, Department of Biochemistry, Laboratory of Molecular Biophysics, South Parks Road, Oxford OX1 3QU, UK.

2. Structural Biology Division, The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, Victoria 3050, Australia.

3. University of Oxford, University Laboratory of Physiology, Parks Road, Oxford OX1 3PT, UK.

4. Department of Microbiology and Bioinformatics, Gifu University Graduate School of Medicine, Regeneration, and Advanced Medical Science, 40 Tsukasamachi, Gifu 500-8705, Japan.

Abstract

The KirBac1.1 channel belongs to the inward-rectifier family of potassium channels. Here we report the structure of the entire prokaryotic Kir channel assembly, in the closed state, refined to a resolution of 3.65 angstroms. We identify the main activation gate and structural elements involved in gating. On the basis of structural evidence presented here, we suggest that gating involves coupling between the intracellular and membrane domains. This further suggests that initiation of gating by membrane or intracellular signals represents different entry points to a common mechanistic pathway.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference30 articles.

1. Ion Channels and Diseases 2000

2. Ionic Channels of Excitable Membranes 2001

3. Materials and Methods are available as supporting material on Science Online.

4. Structural Basis of Inward Rectification

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