3uu8

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The GLIC pentameric Ligand-Gated Ion Channel Loop2-24' mutant reduced in solution

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Retrieved from "http://52.214.119.220/wiki/index.php/3uu8"

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[3uu8]] 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=3UU8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UU8 FirstGlance]. <br>
-</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>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLC:DIUNDECYL+PHOSPHATIDYL+CHOLINE'>PLC</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]] 3.25&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3tls|3tls]], [[3tlt|3tlt]], [[3tlu|3tlu]], [[3tlv|3tlv]], [[3tlw|3tlw]], [[3uu3|3uu3]], [[3uu4|3uu4]], [[3uu5|3uu5]], [[3uu6|3uu6]], [[3uub|3uub]]</div></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>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLC:DIUNDECYL+PHOSPHATIDYL+CHOLINE'>PLC</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glr4197 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=33072 Gloeobacter violaceus])</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=3uu8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uu8 OCA], [https://pdbe.org/3uu8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uu8 RCSB], [https://www.ebi.ac.uk/pdbsum/3uu8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uu8 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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>
+[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;">
-== 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<ref>PMID:22580559</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3uu8" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 29: / Line 19: @@
 [[Category: Gloeobacter violaceus]]
 [[Category: Large Structures]]
-[[Category: Corringer, P J]]
+[[Category: Corringer PJ]]
-[[Category: Delarue, M]]
+[[Category: Delarue M]]
-[[Category: Nury, H]]
+[[Category: Nury H]]
-[[Category: Sauguet, L]]
+[[Category: Sauguet L]]
-[[Category: Cys-loop receptor family]]
-[[Category: Membrane protein]]
-[[Category: Transport protein]]

3uu8

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The GLIC pentameric Ligand-Gated Ion Channel Loop2-24' mutant reduced in solution

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