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CRYSTAL STRUCTURE OF THE RCK DOMAIN FROM E.COLI POTASSIUM CHANNELCRYSTAL STRUCTURE OF THE RCK DOMAIN FROM E.COLI POTASSIUM CHANNEL
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe intracellular C-terminal domain structure of a six-transmembrane K+ channel from Escherichia coli has been solved by X-ray crystallography at 2.4 A 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. Structure of the RCK domain from the E. coli K+ channel and demonstration of its presence in the human BK channel.,Jiang Y, Pico A, Cadene M, Chait BT, MacKinnon R Neuron. 2001 Mar;29(3):593-601. PMID:11301020[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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