Role of the C-terminal domain in the structure and function of tetrameric sodium channels

DOI: 10.1038/ncomms3465
PMID: 24051986

Authors: Claire Bagneris (Birkbeck, University of London) , Paul G. Decaen (Howard Hughes Medical Institute; Harvard Medical School) , Benjamin A. Hall (Microsoft Research Cambridge) , Claire E. Naylor (Birkbeck, University of London) , David E. Clapham (Howard Hughes Medical Institute, Children’s Hospital Boston) , Christopher W. M. Kay (Howard Hughes Medical Institute; Harvard Medical School) , B. A. Wallace (Birkbeck, University of London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 4 , PAGES 7195-7197

State: Published (Approved)
Published: September 2013

Abstract: Voltage-gated sodium channels have essential roles in electrical signalling. Prokaryotic sodium channels are tetramers consisting of transmembrane (TM) voltage-sensing and pore domains, and a cytoplasmic carboxy-terminal domain. Previous crystal structures of bacterial sodium channels revealed the nature of their TM domains but not their C-terminal domains (CTDs). Here, using electron paramagnetic resonance (EPR) spectroscopy combined with molecular dynamics, we show that the CTD of the NavMs channel from Magnetococcus marinus includes a flexible region linking the TM domains to a four-helix coiled-coil bundle.

Journal Keywords: Amino; Bacterial; Crystallography; X-Ray; Electron; Escherichia; Ion;Protein; Secondary; Protein; Tertiary; Recombinant; Static; Voltage-Gated Sodium Channels

Subject Areas: Biology and Bio-materials

Diamond Offline Facilities: Membrane Protein Laboratory (MPL)
Instruments: I02-Macromolecular Crystallography , I04-Macromolecular Crystallography

Other Facilities: Soleil, France (beamline Proxima 1)

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