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

Science, 20 June 2003
Vol. 300, Issue 5627, p. 1922-1926
DOI: 10.1126/science.1085028

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

  1. Anling Kuo1,
  2. Jacqueline M. Gulbis2,
  3. Jennifer F. Antcliff3,
  4. Tahmina Rahman1,
  5. Edward D. Lowe1,
  6. Jochen Zimmer1,
  7. Jonathan Cuthbertson1,
  8. Frances M. Ashcroft3,
  9. Takayuki Ezaki4,
  10. Declan A. Doyle1,*
  1. 1 University of Oxford, Department of Biochemistry, Laboratory of Molecular Biophysics, South Parks Road, Oxford OX1 3QU, UK.
  2. 2 Structural Biology Division, The Walter and Eliza Hall Institute of Medical Research, 1G Royal Parade, Parkville, Victoria 3050, Australia.
  3. 3 University of Oxford, University Laboratory of Physiology, Parks Road, Oxford OX1 3PT, UK.
  4. 4 Department of Microbiology and Bioinformatics, Gifu University Graduate School of Medicine, Regeneration, and Advanced Medical Science, 40 Tsukasamachi, Gifu 500-8705, Japan.
  1. * To whom correspondence should be addressed. E-mail: declan{at}


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.

  • Received for publication 27 March 2003.
  • Accepted for publication 29 April 2003.


A. Kuo, J. M. Gulbis, J. F. Antcliff, T. Rahman, E. D. Lowe, J. Zimmer, J. Cuthbertson, F. M. Ashcroft, T. Ezaki, and D. A. Doyle, Crystal Structure of the Potassium Channel KirBac1.1 in the Closed State. Science 300, 1922-1926 (2003).

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