3uu3: Difference between revisions
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[[ | ==The GLIC pentameric Ligand-Gated Ion Channel Loop2-20' oxidized mutant in a locally-closed conformation (LC1 subtype)== | ||
<StructureSection load='3uu3' size='340' side='right' caption='[[3uu3]], [[Resolution|resolution]] 3.15Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3uu3]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Gloeobacter_violaceus Gloeobacter violaceus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UU3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UU3 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene><br> | |||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tls|3tls]], [[3tlt|3tlt]], [[3tlu|3tlu]], [[3tlv|3tlv]], [[3tlw|3tlw]], [[3uu4|3uu4]], [[3uu5|3uu5]], [[3uu6|3uu6]], [[3uu8|3uu8]], [[3uub|3uub]]</td></tr> | |||
<tr><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 Gloeobacter violaceus])</td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3uu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uu3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3uu3 RCSB], [http://www.ebi.ac.uk/pdbsum/3uu3 PDBsum]</span></td></tr> | |||
<table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | |||
*[[Ion channels|Ion channels]] | |||
== | == References == | ||
[[ | <references/> | ||
__TOC__ | |||
== | </StructureSection> | ||
< | |||
[[Category: Gloeobacter violaceus]] | [[Category: Gloeobacter violaceus]] | ||
[[Category: Corringer, P J.]] | [[Category: Corringer, P J.]] | ||
Revision as of 09:38, 5 June 2014
The GLIC pentameric Ligand-Gated Ion Channel Loop2-20' oxidized mutant in a locally-closed conformation (LC1 subtype)The GLIC pentameric Ligand-Gated Ion Channel Loop2-20' 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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