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Structure of a bacterial voltage-gated sodium channel pore reveals mechanisms of opening and closing

McCusker, Emily C. and Bagneris, Claire and Naylor, Claire E. and Cole, Ambrose R. and d'Avanzo, N. and Nichols, C.G. and Wallace, Bonnie A. (2012) Structure of a bacterial voltage-gated sodium channel pore reveals mechanisms of opening and closing. Nature Communications 3 , ISSN 2041-1723.

Full text not available from this repository.
Official URL: http://dx.doi.org/10.1038/ncomms2077

Abstract

Voltage-gated sodium channels are vital membrane proteins essential for electrical signalling; in humans, they are key targets for the development of pharmaceutical drugs. Here we report the crystal structure of an open-channel conformation of NavMs, the bacterial channel pore from the marine bacterium Magnetococcus sp. (strain MC-1). It differs from the recently published crystal structure of a closed form of a related bacterial sodium channel (NavAb) by having its internal cavity accessible to the cytoplasmic surface as a result of a bend/rotation about a central residue in the carboxy-terminal transmembrane segment. This produces an open activation gate of sufficient diameter to allow hydrated sodium ions to pass through. Comparison of the open and closed structures provides new insight into the features of the functional states present in the activation cycles of sodium channels and the mechanism of channel opening and closing.

Item Type: Article
Keyword(s) / Subject(s): Biological sciences, Biophysics
School or Research Centre: Birkbeck Schools and Research Centres > School of Science > Biological Sciences
Depositing User: Administrator
Date Deposited: 05 Oct 2012 11:37
Last Modified: 17 Apr 2013 12:24
URI: http://eprints.bbk.ac.uk/id/eprint/5170

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