4F4L: Open Channel Conformation Of A Voltage Gated Sodium Channel

Citation:
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.
PDB ID: 4F4LDownload
MMDB ID: 103551
PDB Deposition Date: 2012/5/10
Updated in MMDB: 2012/10
Experimental Method:
x-ray diffraction
Resolution: 3.49  Å
Source Organism:
Similar Structures:
Biological Unit for 4F4L: tetrameric; determined by author and by software (PISA)
Molecular Components in 4F4L
Label Count Molecule
Proteins (4 molecules)
4
Ion Transport Protein
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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