1ID1

CRYSTAL STRUCTURE OF THE RCK DOMAIN FROM E.COLI POTASSIUM CHANNEL

Summary for 1ID1

• Entry DOI: 10.2210/pdb1id1/pdb
• Descriptor: PUTATIVE POTASSIUM CHANNEL PROTEIN (2 entities in total)
• Functional Keywords: rck domain, e.coli potassium channel, bk channel, rossmann fold, membrane protein
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P31069
• Total number of polymer chains: 2
• Total formula weight: 33492.14

Authors

Jiang, Y.,Pico, A.,Cadene, M.,Chait, B.T.,MacKinnon, R. (deposition date: 2001-04-02, release date: 2001-04-11, Last modification date: 2024-02-07)

Primary citation

Jiang, Y.,Pico, A.,Cadene, M.,Chait, B.T.,MacKinnon, R.
Structure of the RCK domain from the E. coli K+ channel and demonstration of its presence in the human BK channel.
Neuron, 29:593-601, 2001

PubMed 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 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.

PubMed: 11301020
DOI: 10.1016/S0896-6273(01)00236-7

Experimental method

X-RAY DIFFRACTION (2.4 Å)