4npp: Difference between revisions
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== | ==The GLIC-His10 wild-type structure in equilibrium between the open and locally-closed (LC) forms== | ||
[[http://www.uniprot.org/uniprot/GLIC_GLOVI GLIC_GLOVI | <StructureSection load='4npp' size='340' side='right'caption='[[4npp]], [[Resolution|resolution]] 3.35Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4npp]] 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=4NPP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NPP FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.35Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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=4npp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4npp OCA], [https://pdbe.org/4npp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4npp RCSB], [https://www.ebi.ac.uk/pdbsum/4npp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4npp 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> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Pentameric ligand-gated ion channels mediate fast chemical transmission of nerve signals. The structure of a bacterial proton-gated homolog has been established in its open and locally closed conformations at acidic pH. Here we report its crystal structure at neutral pH, thereby providing the X-ray structures of the two end-points of the gating mechanism in the same pentameric ligand-gated ion channel. The large structural variability in the neutral pH structure observed in the four copies of the pentamer present in the asymmetric unit has been used to analyze the intrinsic fluctuations in this state, which are found to prefigure the transition to the open state. In the extracellular domain (ECD), a marked quaternary change is observed, involving both a twist and a blooming motion, and the pore in the transmembrane domain (TMD) is closed by an upper bend of helix M2 (as in locally closed form) and a kink of helix M1, both helices no longer interacting across adjacent subunits. On the tertiary level, detachment of inner and outer beta sheets in the ECD reshapes two essential cavities at the ECD-ECD and ECD-TMD interfaces. The first one is the ligand-binding cavity; the other is close to a known divalent cation binding site in other pentameric ligand-gated ion channels. In addition, a different crystal form reveals that the locally closed and open conformations coexist as discrete ones at acidic pH. These structural results, together with site-directed mutagenesis, physiological recordings, and coarse-grained modeling, have been integrated to propose a model of the gating transition pathway. | |||
Crystal structures of a pentameric ligand-gated ion channel provide a mechanism for activation.,Sauguet L, Shahsavar A, Poitevin F, Huon C, Menny A, Nemecz A, Haouz A, Changeux JP, Corringer PJ, Delarue M Proc Natl Acad Sci U S A. 2014 Jan 21;111(3):966-71. doi:, 10.1073/pnas.1314997111. Epub 2013 Dec 23. PMID:24367074<ref>PMID:24367074</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
< | </div> | ||
[[Category: Changeux | <div class="pdbe-citations 4npp" style="background-color:#fffaf0;"></div> | ||
[[Category: Corringer | |||
[[Category: Delarue | ==See Also== | ||
[[Category: Haouz | *[[Ion channels 3D structures|Ion channels 3D structures]] | ||
[[Category: Huon | == References == | ||
[[Category: Menny | <references/> | ||
[[Category: Nemecz | __TOC__ | ||
[[Category: Poitevin | </StructureSection> | ||
[[Category: Sauguet | [[Category: Gloeobacter violaceus PCC 7421]] | ||
[[Category: Shahsavar | [[Category: Large Structures]] | ||
[[Category: Changeux JP]] | |||
[[Category: Corringer PJ]] | |||
[[Category: Delarue M]] | |||
[[Category: Haouz A]] | |||
[[Category: Huon C]] | |||
[[Category: Menny A]] | |||
[[Category: Nemecz A]] | |||
[[Category: Poitevin F]] | |||
[[Category: Sauguet L]] | |||
[[Category: Shahsavar A]] | |||
Latest revision as of 20:01, 20 September 2023
The GLIC-His10 wild-type structure in equilibrium between the open and locally-closed (LC) formsThe GLIC-His10 wild-type structure in equilibrium between the open and locally-closed (LC) forms
Structural highlights
FunctionGLIC_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 PubMedPentameric ligand-gated ion channels mediate fast chemical transmission of nerve signals. The structure of a bacterial proton-gated homolog has been established in its open and locally closed conformations at acidic pH. Here we report its crystal structure at neutral pH, thereby providing the X-ray structures of the two end-points of the gating mechanism in the same pentameric ligand-gated ion channel. The large structural variability in the neutral pH structure observed in the four copies of the pentamer present in the asymmetric unit has been used to analyze the intrinsic fluctuations in this state, which are found to prefigure the transition to the open state. In the extracellular domain (ECD), a marked quaternary change is observed, involving both a twist and a blooming motion, and the pore in the transmembrane domain (TMD) is closed by an upper bend of helix M2 (as in locally closed form) and a kink of helix M1, both helices no longer interacting across adjacent subunits. On the tertiary level, detachment of inner and outer beta sheets in the ECD reshapes two essential cavities at the ECD-ECD and ECD-TMD interfaces. The first one is the ligand-binding cavity; the other is close to a known divalent cation binding site in other pentameric ligand-gated ion channels. In addition, a different crystal form reveals that the locally closed and open conformations coexist as discrete ones at acidic pH. These structural results, together with site-directed mutagenesis, physiological recordings, and coarse-grained modeling, have been integrated to propose a model of the gating transition pathway. Crystal structures of a pentameric ligand-gated ion channel provide a mechanism for activation.,Sauguet L, Shahsavar A, Poitevin F, Huon C, Menny A, Nemecz A, Haouz A, Changeux JP, Corringer PJ, Delarue M Proc Natl Acad Sci U S A. 2014 Jan 21;111(3):966-71. doi:, 10.1073/pnas.1314997111. Epub 2013 Dec 23. PMID:24367074[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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