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Science 300 (5627): 1922-1926

Copyright © 2003 by the American Association for the Advancement of Science

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*

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.

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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   Abstract »    Full Text »    PDF »
The Role of Distal S6 Hydrophobic Residues in the Voltage-dependent Gating of CaV2.3 Channels.
A. Raybaud, E.-E. Baspinar, F. Dionne, Y. Dodier, R. Sauve, and L. Parent (2007)
J. Biol. Chem. 282, 27944-27952
   Abstract »    Full Text »    PDF »
Low-affinity spermine block mediating outward currents through Kir2.1 and Kir2.2 inward rectifier potassium channels.
K. Ishihara and D.-H. Yan (2007)
J. Physiol. 583, 891-908
   Abstract »    Full Text »    PDF »
Crystal structure of a Kir3.1-prokaryotic Kir channel chimera.
M. Nishida, M. Cadene, B. T. Chait, and R. MacKinnon (2007)
EMBO J. 26, 4005-4015
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Impaired interaction between the slide helix and the C-terminus of Kir2.1: A novel mechanism of Andersen syndrome.
N. Decher, V. Renigunta, M. Zuzarte, M. Soom, S. H. Heinemann, K. W. Timothy, M. T. Keating, J. Daut, M. C. Sanguinetti, and I. Splawski (2007)
Cardiovasc Res 75, 748-757
   Abstract »    Full Text »    PDF »
Control of Inward Rectifier K Channel Activity by Lipid Tethering of Cytoplasmic Domains.
D. Enkvetchakul, I. Jeliazkova, J. Bhattacharyya, and C. G. Nichols (2007)
J. Gen. Physiol. 130, 329-334
   Abstract »    Full Text »    PDF »
Identification of the PIP2-binding site on Kir6.2 by molecular modelling and functional analysis.
S. Haider, A. I. Tarasov, T. J. Craig, M. S. Sansom, and F. M. Ashcroft (2007)
EMBO J. 26, 3749-3759
   Abstract »    Full Text »    PDF »

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