Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

8F34

ELIC with Propylamine in spMSP1D1 nanodiscs with 2:1:1 POPC:POPE:POPG

Summary for 8F34
Entry DOI10.2210/pdb8f34/pdb
EMDB information28829 28830 28831 28832 41672 41673
DescriptorErwinia chrysanthemi ligand-gated ion channel, 3-AMINOPROPANE (2 entities in total)
Functional Keywordselic, ion channel, plgic, structural protein, membrane protein, transport protein
Biological sourceDickeya dadantii
Total number of polymer chains5
Total formula weight184690.55
Authors
Dalal, V.,Arcario, M.J.,Petroff II, J.T.,Deitzen, N.M.,Tan, B.K.,Brannigan, G.,Cheng, W.W.L. (deposition date: 2022-11-09, release date: 2023-11-15, Last modification date: 2024-03-27)
Primary citationDalal, V.,Arcario, M.J.,Petroff 2nd, J.T.,Tan, B.K.,Dietzen, N.M.,Rau, M.J.,Fitzpatrick, J.A.J.,Brannigan, G.,Cheng, W.W.L.
Lipid nanodisc scaffold and size alter the structure of a pentameric ligand-gated ion channel.
Nat Commun, 15:25-25, 2024
Cited by
PubMed 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.
PubMed: 38167383
DOI: 10.1038/s41467-023-44366-w
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.12 Å)
Structure validation

237992

数据于2025-06-25公开中

PDB statisticsPDBj update infoContact PDBjnumon