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4zzc

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Revision as of 07:47, 18 May 2023

The GLIC pentameric Ligand-Gated Ion Channel open form complexed to xenon

Structural highlights

4zzc is a 5 chain structure with sequence from Gloeobacter violaceus PCC 7421. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

GLIC receptor is a bacterial pentameric ligand-gated ion channel whose action is inhibited by xenon. Xenon has been used in clinical practice as a potent gaseous anaesthetic for decades, but the molecular mechanism of interactions with its integral membrane receptor targets remains poorly understood. Here we characterize by X-ray crystallography the xenon-binding sites within both the open and "locally-closed" (inactive) conformations of GLIC. Major binding sites of xenon, which differ between the two conformations, were identified in three distinct regions that all belong to the trans-membrane domain of GLIC: 1) in an intra-subunit cavity, 2) at the interface between adjacent subunits, and 3) in the pore. The pore site is unique to the locally-closed form where the binding of xenon effectively seals the channel. A putative mechanism of the inhibition of GLIC by xenon is proposed, which might be extended to other pentameric cationic ligand-gated ion channels.

Structural Basis for Xenon Inhibition in a Cationic Pentameric Ligand-Gated Ion Channel.,Sauguet L, Fourati Z, Prange T, Delarue M, Colloc'h N PLoS One. 2016 Feb 24;11(2):e0149795. doi: 10.1371/journal.pone.0149795., eCollection 2016. PMID:26910105^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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
↑ Sauguet L, Fourati Z, Prange T, Delarue M, Colloc'h N. Structural Basis for Xenon Inhibition in a Cationic Pentameric Ligand-Gated Ion Channel. PLoS One. 2016 Feb 24;11(2):e0149795. doi: 10.1371/journal.pone.0149795., eCollection 2016. PMID:26910105 doi:http://dx.doi.org/10.1371/journal.pone.0149795

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4zzc"

@@ Line 3: / Line 3: @@
 <StructureSection load='4zzc' size='340' side='right'caption='[[4zzc]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4zzc]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Glovi Glovi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZZC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZZC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4zzc]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Gloeobacter_violaceus_PCC_7421 Gloeobacter violaceus PCC 7421]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZZC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZZC FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <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>, <scene name='pdbligand=XE:XENON'>XE</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <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>, <scene name='pdbligand=XE:XENON'>XE</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">glvI, glr4197 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=251221 GLOVI])</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=4zzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zzc OCA], [https://pdbe.org/4zzc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zzc RCSB], [https://www.ebi.ac.uk/pdbsum/4zzc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zzc 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=4zzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zzc OCA], [http://pdbe.org/4zzc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zzc RCSB], [http://www.ebi.ac.uk/pdbsum/4zzc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zzc ProSAT]</span></td></tr>
 </table>
 == 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;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 20: @@
 ==See Also==
-*[[Ion channels|Ion channels]]
+*[[Ion channels 3D structures|Ion channels 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Glovi]]
+[[Category: Gloeobacter violaceus PCC 7421]]
 [[Category: Large Structures]]
-[[Category: Delarue, M]]
+[[Category: Colloc'h N]]
-[[Category: Fourati, Z]]
+[[Category: Delarue M]]
-[[Category: Prange, T]]
+[[Category: Fourati Z]]
-[[Category: Sauguet, L]]
+[[Category: Prange T]]
-[[Category: H, N Colloc]]
+[[Category: Sauguet L]]
-[[Category: Membrane protein]]
-[[Category: Transport protein]]

4zzc

From Proteopedia

Revision as of 07:47, 18 May 2023

The GLIC pentameric Ligand-Gated Ion Channel open form complexed to xenon

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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