期刊
NATURE COMMUNICATIONS
卷 4, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms3465
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资金
- UK Biotechnology and Biological Science Research Council (BBSRC)
- Basic Technology 'Molecular Spintronics' grant from the UK Engineering and Physical Sciences (EPSRC)
- Membrane Protein Laboratory (Diamond Light Source, UK)
- Biotechnology and Biological Sciences Research Council [BB/J020702/1, BB/H01070X/1] Funding Source: researchfish
- BBSRC [BB/J020702/1, BB/H01070X/1] Funding Source: UKRI
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. A 2.9 angstrom resolution crystal structure of the NavMs pore indicates the position of the CTD, which is consistent with the EPR-derived structure. Functional analyses demonstrate that the coiled-coil domain couples inactivation with channel opening, and is enabled by negatively charged residues in the linker region. A mechanism for gating is proposed based on the structure, whereby splaying of the bottom of the pore is possible without requiring unravelling of the coiled-coil.
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