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

DOI: 10.1038/ncomms2077 DOI Help

Authors: Emily Mccusker (Birkbeck College, University of London) , Claire Bagneris (Birkbeck College, University of London) , Claire Naylor (Birkbeck College, University of London) , Ambrose Cole (Birkbeck College, University of London) , Nazzareno D'avanzo (Birkbeck College, University of London) , Colin G. Nichols (Washington University School of Medicine) , B. A. Wallace (Birkbeck, University of London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 3

State: Published (Approved)
Published: October 2012
Diamond Proposal Number(s): 7197

Open Access Open Access

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.

Subject Areas: Biology and Bio-materials

Diamond Offline Facilities: Membrane Protein Laboratory (MPL)
Instruments: I02-Macromolecular Crystallography , I03-Macromolecular Crystallography , I04-Macromolecular Crystallography


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