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

Emily C. McCusker, Claire Bagnéris, Claire E. Naylor, Ambrose R. Cole, Nazzareno D'Avanzo, Colin G. Nichols, B. A. Wallace

Research output: Contribution to journalArticlepeer-review

203 Scopus citations

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.

Original languageEnglish
Article number1102
JournalNature communications
Volume3
DOIs
StatePublished - 2012

Fingerprint Dive into the research topics of 'Structure of a bacterial voltage-gated sodium channel pore reveals mechanisms of opening and closing'. Together they form a unique fingerprint.

Cite this