7JLW

Sheep Connexin-50 at 2.5 angstroms resolution, Lipid Class 1

7JLW の概要

• エントリーDOI: 10.2210/pdb7jlw/pdb
• 関連するPDBエントリー: 7JJP
• EMDBエントリー: 22382
• 分子名称: Gap junction alpha-8 protein, 1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE (3 entities in total)
• 機能のキーワード: connexin, gap junction, lipid, nanodisc, membrane protein
• 由来する生物種: Ovis aries (Sheep)
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 680088.86

構造登録者

Flores, J.A.,Haddad, B.G.,Dolan, K.A.,Myers, J.B.,Yoshioka, C.C.,Copperman, J.,Zuckerman, D.M.,Reichow, S.L. (登録日: 2020-07-30, 公開日: 2020-09-09)

主引用文献

Flores, J.A.,Haddad, B.G.,Dolan, K.A.,Myers, J.B.,Yoshioka, C.C.,Copperman, J.,Zuckerman, D.M.,Reichow, S.L.
Connexin-46/50 in a dynamic lipid environment resolved by CryoEM at 1.9 angstrom.
Nat Commun, 11:4331-4331, 2020

PubMed Abstract: Gap junctions establish direct pathways for cells to transfer metabolic and electrical messages. The local lipid environment is known to affect the structure, stability and intercellular channel activity of gap junctions; however, the molecular basis for these effects remains unknown. Here, we incorporate native connexin-46/50 (Cx46/50) intercellular channels into a dual lipid nanodisc system, mimicking a native cell-to-cell junction. Structural characterization by CryoEM reveals a lipid-induced stabilization to the channel, resulting in a 3D reconstruction at 1.9 Å resolution. Together with all-atom molecular dynamics simulations, it is shown that Cx46/50 in turn imparts long-range stabilization to the dynamic local lipid environment that is specific to the extracellular lipid leaflet. In addition, ~400 water molecules are resolved in the CryoEM map, localized throughout the intercellular permeation pathway and contributing to the channel architecture. These results illustrate how the aqueous-lipid environment is integrated with the architectural stability, structure and function of gap junction communication channels.

PubMed: 32859914
DOI: 10.1038/s41467-020-18120-5

実験手法

ELECTRON MICROSCOPY (2.5 Å)