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Originally published in Science Express on 8 May 2003
Science 20 June 2003:
Vol. 300. no. 5627, pp. 1922 - 1926
DOI: 10.1126/science.1085028
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Research Articles

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

Anling Kuo,1 Jacqueline M. Gulbis,2 Jennifer F. Antcliff,3 Tahmina Rahman,1 Edward D. Lowe,1 Jochen Zimmer,1 Jonathan Cuthbertson,1 Frances M. Ashcroft,3 Takayuki Ezaki,4 Declan A. Doyle1*

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.

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.

* To whom correspondence should be addressed. E-mail: declan{at}biop.ox.ac.uk

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