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-Structure paper
Title | Lipid nanodisc scaffold and size alter the structure of a pentameric ligand-gated ion channel. |
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Journal, issue, pages | Nat Commun, Vol. 15, Issue 1, Page 25, Year 2024 |
Publish date | Jan 2, 2024 |
Authors | Vikram Dalal / Mark J Arcario / John T Petroff / Brandon K Tan / Noah M Dietzen / Michael J Rau / James A J Fitzpatrick / Grace Brannigan / Wayland W L Cheng / |
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 ...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. |
External links | Nat Commun / PubMed:38167383 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.12 - 3.71 Å |
Structure data | EMDB-28829, PDB-8f32: EMDB-28830, PDB-8f33: EMDB-28831, PDB-8f34: EMDB-28832, PDB-8f35: EMDB-41672, PDB-8twv: EMDB-41673, PDB-8twz: |
Chemicals | ChemComp-3CN: |
Source |
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Keywords | TRANSPORT PROTEIN / ELIC / ion channel / pLGIC / Structural Protein / Membrane Protein |