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Nature 440, 570-574 (23 March 2006) | doi:10.1038/nature04508; Received 28 July 2005; Accepted 5 December 2005; Published online 8 February 2006

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Atomic structure of a Na+- and K+-conducting channel

Ning Shi1, Sheng Ye1, Amer Alam1, Liping Chen1 & Youxing Jiang1

  1. Department of Physiology, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9040, USA

Correspondence to: Youxing Jiang1 Correspondence and requests for materials should be addressed to Y.J. (Email: youxing.jiang@utsouthwestern.edu). Atomic coordinates of the Na+ and K+ complexes of the NaK channel have been deposited in the Protein Data Bank with accession numbers of 2AHY and 2AHZ, respectively.

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Ion selectivity is one of the basic properties that define an ion channel. Most tetrameric cation channels, which include the K+, Ca2+, Na+ and cyclic nucleotide-gated channels, probably share a similar overall architecture in their ion-conduction pore, but the structural details that determine ion selection are different. Although K+ channel selectivity has been well studied from a structural perspective1, 2, little is known about the structure of other cation channels. Here we present crystal structures of the NaK channel from Bacillus cereus, a non-selective tetrameric cation channel, in its Na+- and K+-bound states at 2.4 Å and 2.8 Å resolution, respectively. The NaK channel shares high sequence homology and a similar overall structure with the bacterial KcsA K+ channel, but its selectivity filter adopts a different architecture. Unlike a K+ channel selectivity filter, which contains four equivalent K+-binding sites, the selectivity filter of the NaK channel preserves the two cation-binding sites equivalent to sites 3 and 4 of a K+ channel, whereas the region corresponding to sites 1 and 2 of a K+ channel becomes a vestibule in which ions can diffuse but not bind specifically. Functional analysis using an 86Rb flux assay shows that the NaK channel can conduct both Na+ and K+ ions. We conclude that the sequence of the NaK selectivity filter resembles that of a cyclic nucleotide-gated channel and its structure may represent that of a cyclic nucleotide-gated channel pore.

  1. Department of Physiology, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9040, USA

Correspondence to: Youxing Jiang1 Correspondence and requests for materials should be addressed to Y.J. (Email: youxing.jiang@utsouthwestern.edu). Atomic coordinates of the Na+ and K+ complexes of the NaK channel have been deposited in the Protein Data Bank with accession numbers of 2AHY and 2AHZ, respectively.

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