EMD-28830
ELIC with Propylamine in saposin nanodiscs with 2:1:1 POPC:POPE:POPG
EMD-28830
Single-particle3.28 Å

Map released: 15/11/2023
Last modified: 27/03/2024
Sample Organism:
Dickeya dadantii
Sample: ELIC with Propylamine in saposin nanodiscs with 2:1:1 POPC:POPE:POPG
Fitted models: 8f33 (Avg. Q-score: 0.496)
Deposition Authors: Dalal V
,
Arcario MJ
,
Petroff II JT
,
Deitzen NM,
Tan BK,
Brannigan G
,
Cheng WWL
Sample: ELIC with Propylamine in saposin nanodiscs with 2:1:1 POPC:POPE:POPG
Fitted models: 8f33 (Avg. Q-score: 0.496)
Deposition Authors: Dalal V





Lipid nanodisc scaffold and size alter the structure of a pentameric ligand-gated ion channel.
Dalal V
,
Arcario MJ
,
Petroff 2nd JT,
Tan BK,
Dietzen NM,
Rau MJ
,
Fitzpatrick JAJ,
Brannigan G
,
Cheng WWL
(2024) Nat Commun , 15 , 25 - 25





(2024) Nat Commun , 15 , 25 - 25
Abstract:
Lipid nanodiscs have become a standard tool for studying membrane proteins, including using single particle cryo-electron microscopy (cryo-EM). We find that reconstituting the pentameric ligand-gated ion channel (pLGIC), Erwinia ligand-gated ion channel (ELIC), in different nanodiscs produces distinct structures by cryo-EM. The effect of the nanodisc on ELIC structure extends to the extracellular domain and agonist binding site. Additionally, molecular dynamic simulations indicate that nanodiscs of different size impact ELIC structure and that the nanodisc scaffold directly interacts with ELIC. These findings suggest that the nanodisc plays a crucial role in determining the structure of pLGICs, and that reconstitution of ion channels in larger nanodiscs may better approximate a lipid membrane environment.
Lipid nanodiscs have become a standard tool for studying membrane proteins, including using single particle cryo-electron microscopy (cryo-EM). We find that reconstituting the pentameric ligand-gated ion channel (pLGIC), Erwinia ligand-gated ion channel (ELIC), in different nanodiscs produces distinct structures by cryo-EM. The effect of the nanodisc on ELIC structure extends to the extracellular domain and agonist binding site. Additionally, molecular dynamic simulations indicate that nanodiscs of different size impact ELIC structure and that the nanodisc scaffold directly interacts with ELIC. These findings suggest that the nanodisc plays a crucial role in determining the structure of pLGICs, and that reconstitution of ion channels in larger nanodiscs may better approximate a lipid membrane environment.