7Q3H

Pentameric ligand-gated ion channel, DeCLIC at pH 7 with 10 mM EDTA

7Q3H の概要

• エントリーDOI: 10.2210/pdb7q3h/pdb
• 関連するPDBエントリー: 7Q3G
• EMDBエントリー: 13791 13792
• 分子名称: Neur_chan_LBD domain-containing protein (1 entity in total)
• 機能のキーワード: ion channel, ligand-gated channel, pentameric channel, membrane protein
• 由来する生物種: Desulfofustis sp. PB-SRB1
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 358669.96

構造登録者

Lycksell, M.,Rovsnik, U.,Hanke, A.,Howard, R.J.,Lindahl, E. (登録日: 2021-10-27, 公開日: 2022-11-16, 最終更新日: 2025-07-09)

主引用文献

Lycksell, M.,Rovsnik, U.,Hanke, A.,Martel, A.,Howard, R.J.,Lindahl, E.
Biophysical characterization of calcium-binding and modulatory-domain dynamics in a pentameric ligand-gated ion channel.
Proc.Natl.Acad.Sci.USA, 119:e2210669119-e2210669119, 2022

PubMed Abstract: Pentameric ligand-gated ion channels (pLGICs) perform electrochemical signal transduction in organisms ranging from bacteria to humans. Among the prokaryotic pLGICs, there is architectural diversity involving N-terminal domains (NTDs) not found in eukaryotic relatives, exemplified by the calcium-sensitive channel (DeCLIC) from a deltaproteobacterium, which has an NTD in addition to the canonical pLGIC structure. Here, we have characterized the structure and dynamics of DeCLIC through cryoelectron microscopy (cryo-EM), small-angle neutron scattering (SANS), and molecular dynamics (MD) simulations. In the presence and absence of calcium, cryo-EM yielded structures with alternative conformations of the calcium-binding site. SANS profiles further revealed conformational diversity at room temperature beyond that observed in static structures, shown through MD to be largely attributable to rigid-body motions of the NTD relative to the protein core, with expanded and asymmetric conformations improving the fit of the SANS data. This work reveals the range of motion available to the DeCLIC NTD and calcium-binding site, expanding the conformational landscape of the pLGIC family. Further, these findings demonstrate the power of combining low-resolution scattering, high-resolution structural, and MD simulation data to elucidate interfacial interactions that are highly conserved in the pLGIC family.

PubMed: 36480474
DOI: 10.1073/pnas.2210669119

実験手法

ELECTRON MICROSCOPY (3.2 Å)