7PGF

Calcium-selective Sp1 channel pore domain only

7PGF の概要

• エントリーDOI: 10.2210/pdb7pgf/pdb
• 関連するPDBエントリー: 7PG8 7PGP
• 分子名称: Ion transporter (1 entity in total)
• 機能のキーワード: ion channel membrane protein transport protein antibody complex, membrane protein
• 由来する生物種: Ruegeria pomeroyi
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31025.91

構造登録者

Lolicato, M.,Arrigoni, C. (登録日: 2021-08-13, 公開日: 2022-06-08, 最終更新日: 2024-06-19)

主引用文献

Arrigoni, C.,Lolicato, M.,Shaya, D.,Rohaim, A.,Findeisen, F.,Fong, L.K.,Colleran, C.M.,Dominik, P.,Kim, S.S.,Schuermann, J.P.,DeGrado, W.F.,Grabe, M.,Kossiakoff, A.A.,Minor Jr., D.L.
Quaternary structure independent folding of voltage-gated ion channel pore domain subunits.
Nat.Struct.Mol.Biol., 29:537-548, 2022

PubMed Abstract: Every voltage-gated ion channel (VGIC) has a pore domain (PD) made from four subunits, each comprising an antiparallel transmembrane helix pair bridged by a loop. The extent to which PD subunit structure requires quaternary interactions is unclear. Here, we present crystal structures of a set of bacterial voltage-gated sodium channel (BacNa) 'pore only' proteins that reveal a surprising collection of non-canonical quaternary arrangements in which the PD tertiary structure is maintained. This context-independent structural robustness, supported by molecular dynamics simulations, indicates that VGIC-PD tertiary structure is independent of quaternary interactions. This fold occurs throughout the VGIC superfamily and in diverse transmembrane and soluble proteins. Strikingly, characterization of PD subunit-binding Fabs indicates that non-canonical quaternary PD conformations can occur in full-length VGICs. Together, our data demonstrate that the VGIC-PD is an autonomously folded unit. This property has implications for VGIC biogenesis, understanding functional states, de novo channel design, and VGIC structural origins.

PubMed: 35655098
DOI: 10.1038/s41594-022-00775-x

実験手法

X-RAY DIFFRACTION (3.5 Å)