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9NH4

ELIC with propylamine in spNW25 nanodiscs with 2:1:1 POPC:POPE:POPG

Summary for 9NH4
Entry DOI10.2210/pdb9nh4/pdb
EMDB information49400
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.,Cheng, W.W.L. (deposition date: 2025-02-23, release date: 2025-07-23, Last modification date: 2025-07-30)
Primary citationDalal, V.,Tan, B.K.,Xu, H.,Cheng, W.W.L.
Cryo-EM structures of a pentameric ligand-gated ion channel in liposomes.
Elife, 14:-, 2025
Cited by
PubMed Abstract: Detergents and lipid nanodiscs affect the cryo-EM structures of pentameric ligand-gated ion channels (pLGICs) including ELIC. To determine the structure of a pLGIC in a membrane environment that supports ion channel function, we performed single particle cryo-EM of ELIC in liposomes. ELIC activation and desensitization were confirmed in liposomes with a stopped-flow thallium flux assay. Using WT ELIC and a non-desensitizing mutant (ELIC5), we captured resting, activated, and desensitized structures at high resolution. In the desensitized structure, the ion conduction pore has a constriction at the 9' leucine of the pore-lining M2 helix, indicating that 9' is the desensitization gate in ELIC. The agonist-bound structures of ELIC in liposomes are distinct from those in nanodiscs. In general, the transmembrane domain is more loosely packed in liposomes compared to nanodiscs. It has been suggested that large nanodiscs are superior for supporting membrane protein function. However, ELIC localizes to the rim of large circularized nanodiscs, and structures of ELIC in large nanodiscs deviate from the liposome structures more than those in small nanodiscs. Using liposomes for cryo-EM structure determination of a pLGIC increases our confidence that the structures are snapshots of functional states.
PubMed: 40668221
DOI: 10.7554/eLife.106728
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.9 Å)
Structure validation

239492

數據於2025-07-30公開中

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