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

Nature. 2006 Mar 23;440(7083):570-4. doi: 10.1038/nature04508. Epub 2006 Feb 8.

Abstract

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 perspective, 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 A and 2.8 A 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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Bacillus cereus / chemistry*
  • Bacillus cereus / metabolism
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Crystallography, X-Ray
  • Liposomes
  • Models, Molecular
  • Potassium / metabolism
  • Potassium Channels / chemistry*
  • Potassium Channels / metabolism
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Rubidium / metabolism
  • Sodium / metabolism
  • Sodium Channels / chemistry*
  • Sodium Channels / metabolism

Substances

  • Bacterial Proteins
  • Liposomes
  • Potassium Channels
  • Recombinant Proteins
  • Sodium Channels
  • prokaryotic potassium channel
  • Sodium
  • Rubidium
  • Potassium

Associated data

  • PDB/2AHY
  • PDB/2AHZ