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| | ==The GLIC pentameric Ligand-Gated Ion Channel Loop2-21' oxidized mutant in a locally-closed conformation (LC2 subtype)== | | ==The GLIC pentameric Ligand-Gated Ion Channel Loop2-21' oxidized mutant in a locally-closed conformation (LC2 subtype)== |
| - | <StructureSection load='3tlw' size='340' side='right' caption='[[3tlw]], [[Resolution|resolution]] 2.60Å' scene=''> | + | <StructureSection load='3tlw' size='340' side='right'caption='[[3tlw]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3tlw]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Glovo Glovo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TLW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TLW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3tlw]] 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=3TLW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TLW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tls|3tls]], [[3tlt|3tlt]], [[3tlu|3tlu]], [[3tlv|3tlv]]</td></tr> | + | <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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glr4197 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=33072 GLOVO])</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=3tlw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tlw OCA], [https://pdbe.org/3tlw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tlw RCSB], [https://www.ebi.ac.uk/pdbsum/3tlw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tlw ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3tlw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tlw OCA], [http://pdbe.org/3tlw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tlw RCSB], [http://www.ebi.ac.uk/pdbsum/3tlw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3tlw ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GLIC_GLOVI GLIC_GLOVI]] Cationic channel with similar permeabilities for Na(+) and K(+), that is activated by an increase of the proton concentration on the extracellular side. Displays no permeability for chloride ions. Shows slow kinetics of activation, no desensitization and a single channel conductance of 8 pS. Might contribute to adaptation to external pH change.<ref>PMID:17167423</ref> | + | [https://www.uniprot.org/uniprot/GLIC_GLOVI GLIC_GLOVI] Cationic channel with similar permeabilities for Na(+) and K(+), that is activated by an increase of the proton concentration on the extracellular side. Displays no permeability for chloride ions. Shows slow kinetics of activation, no desensitization and a single channel conductance of 8 pS. Might contribute to adaptation to external pH change.<ref>PMID:17167423</ref> |
| | <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: Glovo]] | + | [[Category: Gloeobacter violaceus]] |
| - | [[Category: Corringer, P J]] | + | [[Category: Large Structures]] |
| - | [[Category: Delarue, M]] | + | [[Category: Corringer PJ]] |
| - | [[Category: Nury, H]] | + | [[Category: Delarue M]] |
| - | [[Category: Sauguet, L]] | + | [[Category: Nury H]] |
| - | [[Category: Cys-loop receptor family]]
| + | [[Category: Sauguet L]] |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
GLIC_GLOVI Cationic channel with similar permeabilities for Na(+) and K(+), that is activated by an increase of the proton concentration on the extracellular side. Displays no permeability for chloride ions. Shows slow kinetics of activation, no desensitization and a single channel conductance of 8 pS. Might contribute to adaptation to external pH change.[1]
Publication Abstract from PubMed
Pentameric 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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bocquet N, Prado de Carvalho L, Cartaud J, Neyton J, Le Poupon C, Taly A, Grutter T, Changeux JP, Corringer PJ. A prokaryotic proton-gated ion channel from the nicotinic acetylcholine receptor family. Nature. 2007 Jan 4;445(7123):116-9. Epub 2006 Dec 10. PMID:17167423 doi:10.1038/nature05371
- ↑ Prevost MS, Sauguet L, Nury H, Van Renterghem C, Huon C, Poitevin F, Baaden M, Delarue M, Corringer PJ. A locally closed conformation of a bacterial pentameric proton-gated ion channel. Nat Struct Mol Biol. 2012 May 13. doi: 10.1038/nsmb.2307. PMID:22580559 doi:10.1038/nsmb.2307
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