3tlu: Difference between revisions
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==The GLIC pentameric Ligand-Gated Ion Channel Loop2-24' oxidized mutant in a locally-closed conformation (LC1 subtype)== | ==The GLIC pentameric Ligand-Gated Ion Channel Loop2-24' oxidized mutant in a locally-closed conformation (LC1 subtype)== | ||
<StructureSection load='3tlu' size='340' side='right' caption='[[3tlu]], [[Resolution|resolution]] 2.85Å' scene=''> | <StructureSection load='3tlu' size='340' side='right'caption='[[3tlu]], [[Resolution|resolution]] 2.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3tlu]] is a 5 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3tlu]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Gloeobacter_violaceus Gloeobacter violaceus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TLU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TLU FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</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=3tlu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tlu OCA], [https://pdbe.org/3tlu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tlu RCSB], [https://www.ebi.ac.uk/pdbsum/3tlu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tlu ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Ion channels|Ion channels]] | *[[Ion channels 3D structures|Ion channels 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Gloeobacter violaceus]] | ||
[[Category: Corringer | [[Category: Large Structures]] | ||
[[Category: Delarue | [[Category: Corringer PJ]] | ||
[[Category: Nury | [[Category: Delarue M]] | ||
[[Category: Sauguet | [[Category: Nury H]] | ||
[[Category: Sauguet L]] | |||
Latest revision as of 05:27, 21 November 2024
The GLIC pentameric Ligand-Gated Ion Channel Loop2-24' oxidized mutant in a locally-closed conformation (LC1 subtype)The GLIC pentameric Ligand-Gated Ion Channel Loop2-24' oxidized mutant in a locally-closed conformation (LC1 subtype)
Structural highlights
Publication Abstract from PubMedPentameric ligand-gated ion channels mediate signal transduction through conformational transitions between closed-pore and open-pore states. To stabilize a closed conformation of GLIC, a bacterial proton-gated homolog from Gloeobacter violaceus whose open structure is known, we separately generated either four cross-links or two single mutations. We found all six mutants to be in the same 'locally closed' conformation using X-ray crystallography, sharing most of the features of the open form but showing a locally closed pore as a result of a concerted bending of all of its M2 helices. The mutants adopt several variant conformations of the M2-M3 loop, and in all cases an interacting lipid that is observed in the open form disappears. A single cross-linked mutant is functional, according to electrophysiology, and the locally closed structure of this mutant indicates that it has an increased flexibility. Further cross-linking, accessibility and molecular dynamics data suggest that the locally closed form is a functionally relevant conformation that occurs during allosteric gating transitions. A locally closed conformation of a bacterial pentameric proton-gated ion channel.,Prevost MS, Sauguet L, Nury H, Van Renterghem C, Huon C, Poitevin F, Baaden M, Delarue M, Corringer PJ Nat Struct Mol Biol. 2012 May 13. doi: 10.1038/nsmb.2307. PMID:22580559[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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