8d66: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[8d66]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Dickeya_dadantii Dickeya dadantii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8D66 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8D66 FirstGlance]. <br> | <table><tr><td colspan='2'>[[8d66]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Dickeya_dadantii Dickeya dadantii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8D66 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8D66 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DHL:2-AMINO-ETHANETHIOL'>DHL</scene>, <scene name='pdbligand=PGW:(1R)-2-{[(S)-{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(HEXADECANOYLOXY)METHYL]ETHYL+(9Z)-OCTADEC-9-ENOATE'>PGW</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.14Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DHL:2-AMINO-ETHANETHIOL'>DHL</scene>, <scene name='pdbligand=PGW:(1R)-2-{[(S)-{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(HEXADECANOYLOXY)METHYL]ETHYL+(9Z)-OCTADEC-9-ENOATE'>PGW</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8d66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8d66 OCA], [https://pdbe.org/8d66 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8d66 RCSB], [https://www.ebi.ac.uk/pdbsum/8d66 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8d66 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8d66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8d66 OCA], [https://pdbe.org/8d66 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8d66 RCSB], [https://www.ebi.ac.uk/pdbsum/8d66 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8d66 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/E0SJQ4_DICD3 E0SJQ4_DICD3] | [https://www.uniprot.org/uniprot/E0SJQ4_DICD3 E0SJQ4_DICD3] | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
Open-channel structure of a pentameric ligand-gated ion channel reveals a mechanism of leaflet-specific phospholipid modulation.,Petroff JT 2nd, Dietzen NM, Santiago-McRae E, Deng B, Washington MS, Chen LJ, Trent Moreland K, Deng Z, Rau M, Fitzpatrick JAJ, Yuan P, Joseph TT, Henin J, Brannigan G, Cheng WWL Nat Commun. 2022 Nov 17;13(1):7017. doi: 10.1038/s41467-022-34813-5. PMID:36385237<ref>PMID:36385237</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 8d66" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ion channels 3D structures|Ion channels 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 08:19, 12 June 2024
ELIC with cysteamine in 2:1:1 POPC:POPE:POPG nanodiscELIC with cysteamine in 2:1:1 POPC:POPE:POPG nanodisc
Structural highlights
FunctionPublication Abstract from PubMedPentameric 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. Open-channel structure of a pentameric ligand-gated ion channel reveals a mechanism of leaflet-specific phospholipid modulation.,Petroff JT 2nd, Dietzen NM, Santiago-McRae E, Deng B, Washington MS, Chen LJ, Trent Moreland K, Deng Z, Rau M, Fitzpatrick JAJ, Yuan P, Joseph TT, Henin J, Brannigan G, Cheng WWL Nat Commun. 2022 Nov 17;13(1):7017. doi: 10.1038/s41467-022-34813-5. PMID:36385237[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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