6hk0

X-ray structure of a pentameric ligand gated ion channel from Erwinia chrysanthemi (ELIC) F16'S pore mutant (F247S) with alternate M4 conformation.

spinqualitylabelsall models 6hk0, resolution 3.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6hk0 is a 10 chain structure with sequence from "erwinia_carotovora_var._chrysanthemi"_(burkholder_et_al._1953)_dye_1969 "erwinia carotovora var. chrysanthemi" (burkholder et al. 1953) dye 1969. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: LMT Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Phospholipids are key components of cellular membranes and are emerging as important functional regulators of different membrane proteins, including pentameric ligand-gated ion channels (pLGICs). Here, we take advantage of the prokaryote channel ELIC (Erwinia ligand-gated ion channel) as a model to understand the determinants of phospholipid interactions in this family of receptors. A high-resolution structure of ELIC in a lipid-bound state reveals a phospholipid site at the lower half of pore-forming transmembrane helices M1 and M4 and at a nearby site for neurosteroids, cholesterol or general anesthetics. This site is shaped by an M4-helix kink and a Trp-Arg-Pro triad that is highly conserved in eukaryote GABAA/C and glycine receptors. A combined approach reveals that M4 is intrinsically flexible and that M4 deletions or disruptions of the lipid-binding site accelerate desensitization in ELIC, suggesting that lipid interactions shape the agonist response. Our data offer a structural context for understanding lipid modulation in pLGICs. A lipid site shapes the agonist response of a pentameric ligand-gated ion channel.,Henault CM, Govaerts C, Spurny R, Brams M, Estrada-Mondragon A, Lynch J, Bertrand D, Pardon E, Evans GL, Woods K, Elberson BW, Cuello LG, Brannigan G, Nury H, Steyaert J, Baenziger JE, Ulens C Nat Chem Biol. 2019 Oct 7. pii: 10.1038/s41589-019-0369-4. doi:, 10.1038/s41589-019-0369-4. PMID:31591563 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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