Structure of the RCK domain from the E. coli K+ channel and demonstration of its presence in the human BK channel

Youxing Jiang, Alexander Pico, Martine Cadene, Brian T. Chait, Roderick MacKinnon

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238 Scopus citations

Abstract

The intracellular C-terminal domain structure of a six-transmembrane K+ channel from Escherichia coli has been solved by X-ray crystallography at 2.4 Å resolution. The structure is representative of a broad class of domains/proteins that regulate the conductance of K+ (here referred to as RCK domains) in prokaryotic K+ transporters and K+ channels. The RCK domain has a Rossmann-fold topology with unique positions, not commonly conserved among Rossmann-fold proteins, composing a well-conserved salt bridge and a hydrophobic dimer interface. Structure-based amino acid sequence alignments and mutational analysis are used to demonstrate that an RCK domain is also present and is an important component of the gating machinery in eukaryotic large-conductance Ca2+-activated K+ channels.

Original languageEnglish (US)
Pages (from-to)593-601
Number of pages9
JournalNeuron
Volume29
Issue number3
DOIs
Publication statusPublished - 2001

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ASJC Scopus subject areas

  • Neuroscience(all)

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