5HVX

Full length Wild-Type Open-form Sodium Channel NavMs

5HVX の概要

• エントリーDOI: 10.2210/pdb5hvx/pdb
• 分子名称: Ion transport protein, SODIUM ION, HEGA-10, ... (7 entities in total)
• 機能のキーワード: integral membrane full length voltage gated sodium channel transport, transport protein
• 由来する生物種: Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32667.39

構造登録者

Sula, A.,Booker, J.E.,Naylor, C.E.,Wallace, B.A. (登録日: 2016-01-28, 公開日: 2017-03-01, 最終更新日: 2024-01-10)

主引用文献

Sula, A.,Booker, J.,Ng, L.C.,Naylor, C.E.,DeCaen, P.G.,Wallace, B.A.
The complete structure of an activated open sodium channel.
Nat Commun, 8:14205-14205, 2017

PubMed Abstract: Voltage-gated sodium channels (Navs) play essential roles in excitable tissues, with their activation and opening resulting in the initial phase of the action potential. The cycling of Navs through open, closed and inactivated states, and their closely choreographed relationships with the activities of other ion channels lead to exquisite control of intracellular ion concentrations in both prokaryotes and eukaryotes. Here we present the 2.45 Å resolution crystal structure of the complete NavMs prokaryotic sodium channel in a fully open conformation. A canonical activated conformation of the voltage sensor S4 helix, an open selectivity filter leading to an open activation gate at the intracellular membrane surface and the intracellular C-terminal domain are visible in the structure. It includes a heretofore unseen interaction motif between W77 of S3, the S4-S5 interdomain linker, and the C-terminus, which is associated with regulation of opening and closing of the intracellular gate.

PubMed: 28205548
DOI: 10.1038/ncomms14205

実験手法

X-RAY DIFFRACTION (2.45 Å)