Summary for 8VUW
| Entry DOI | 10.2210/pdb8vuw/pdb |
| Related | 8D63 8D64 8D65 8D66 8D67 |
| EMDB information | 27215 27216 27217 27218 27219 43542 |
| Descriptor | Erwinia chrysanthemi ligand-gated ion channel, (1R)-2-{[(S)-{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(hexadecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate, 2-AMINO-ETHANETHIOL (3 entities in total) |
| Functional Keywords | elic, ion channel, plgic, transport protein |
| Biological source | Dickeya chrysanthemi (Pectobacterium chrysanthemi, Erwinia chrysanthemi) |
| Total number of polymer chains | 5 |
| Total formula weight | 189186.05 |
| Authors | Petroff II, J.T.,Deng, Z.,Rau, M.J.,Fitzpatrick, J.A.J.,Yuan, P.,Cheng, W.W.L. (deposition date: 2024-01-29, release date: 2024-02-07) |
| Primary citation | Petroff, J.T.,Dietzen, N.M.,Santiago-McRae, E.,Deng, B.,Washington, M.S.,Chen, L.J.,Trent Moreland, K.,Deng, Z.,Rau, M.,Fitzpatrick, J.A.J.,Yuan, P.,Joseph, T.T.,Henin, J.,Brannigan, G.,Cheng, W.W.L. Open-channel structure of a pentameric ligand-gated ion channel reveals a mechanism of leaflet-specific phospholipid modulation. Nat Commun, 13:7017-, 2022 Cited by PubMed Abstract: Pentameric ligand-gated ion channels (pLGICs) mediate synaptic transmission and are sensitive to their lipid environment. The mechanism of phospholipid modulation of any pLGIC is not well understood. We demonstrate that the model pLGIC, ELIC (Erwinia ligand-gated ion channel), is positively modulated by the anionic phospholipid, phosphatidylglycerol, from the outer leaflet of the membrane. To explore the mechanism of phosphatidylglycerol modulation, we determine a structure of ELIC in an open-channel conformation. The structure shows a bound phospholipid in an outer leaflet site, and structural changes in the phospholipid binding site unique to the open-channel. In combination with streamlined alchemical free energy perturbation calculations and functional measurements in asymmetric liposomes, the data support a mechanism by which an anionic phospholipid stabilizes the activated, open-channel state of a pLGIC by specific, state-dependent binding to this site. PubMed: 36385237DOI: 10.1038/s41467-022-34813-5 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.19 Å) |
Structure validation
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