4F4L

Open Channel Conformation of a Voltage Gated Sodium Channel

Summary for 4F4L

• Entry DOI: 10.2210/pdb4f4l/pdb
• Descriptor: Ion transport protein (2 entities in total)
• Functional Keywords: alpha helical membrane protein, voltage-gated sodium channel, membrane, metal transport
• Biological source: Magnetococcus marinus
• Total number of polymer chains: 4
• Total formula weight: 49758.06

Authors

McCusker, E.C.,Bagneris, C.,Naylor, C.E.,Cole, A.R.,D'Avanzo, N.,Nichols, C.G.,Wallace, B.A. (deposition date: 2012-05-10, release date: 2012-10-03, Last modification date: 2023-09-13)

Primary citation

McCusker, E.C.,Bagneris, C.,Naylor, C.E.,Cole, A.R.,D'Avanzo, N.,Nichols, C.G.,Wallace, B.A.
Structure of a bacterial voltage-gated sodium channel pore reveals mechanisms of opening and closing.
Nat Commun, 3:1102-1102, 2012

PubMed 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.

PubMed: 23033078
DOI: 10.1038/ncomms2077

Experimental method

X-RAY DIFFRACTION (3.49 Å)