4F4L

Open Channel Conformation of a Voltage Gated Sodium Channel

4F4L の概要

• エントリーDOI: 10.2210/pdb4f4l/pdb
• 分子名称: Ion transport protein (2 entities in total)
• 機能のキーワード: alpha helical membrane protein, voltage-gated sodium channel, membrane, metal transport
• 由来する生物種: Magnetococcus marinus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 49758.06

構造登録者

McCusker, E.C.,Bagneris, C.,Naylor, C.E.,Cole, A.R.,D'Avanzo, N.,Nichols, C.G.,Wallace, B.A. (登録日: 2012-05-10, 公開日: 2012-10-03, 最終更新日: 2023-09-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.49 Å)