7pa0: Difference between revisions
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==NaK C-DI F92A mutant with Rb+ and K+== | ==NaK C-DI F92A mutant with Rb+ and K+== | ||
<StructureSection load='7pa0' size='340' side='right'caption='[[7pa0]]' scene=''> | <StructureSection load='7pa0' size='340' side='right'caption='[[7pa0]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PA0 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7pa0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus_ATCC_14579 Bacillus cereus ATCC 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PA0 FirstGlance]. <br> | ||
</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=7pa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pa0 OCA], [https://pdbe.org/7pa0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pa0 RCSB], [https://www.ebi.ac.uk/pdbsum/7pa0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pa0 ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=RB:RUBIDIUM+ION'>RB</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=7pa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pa0 OCA], [https://pdbe.org/7pa0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pa0 RCSB], [https://www.ebi.ac.uk/pdbsum/7pa0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pa0 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q81HW2_BACCR Q81HW2_BACCR] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Ionotropic glutamate receptors are ligand-gated cation channels that play essential roles in the excitatory synaptic transmission throughout the central nervous system. A number of open-pore structures of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic-acid (AMPA)-type glutamate receptors became recently available by cryo-electron microscopy (cryo-EM). These structures provide valuable insights into the conformation of the selectivity filter (SF), the part of the ion channel that determines the ion selectivity. Nonetheless, due to the moderate resolution of the cryo-EM structures, detailed information such as ion occupancy of monovalent and divalent cations as well as exact displacement of the side-chains in the SF is still missing. Here, in an attempt to obtain high-resolution information about glutamate receptor SFs, we incorporated partial SF sequences of the AMPA and kainate receptors into the bacterial tetrameric cation channel NaK, which served as a structural scaffold. We determined a series of X-ray structures of NaK-CDI, NaK-SDI and NaK-SELM mutants at 1.42-2.10 A resolution, showing distinct ion occupation of different monovalent cations. Molecular dynamics (MD) simulations of NaK-CDI indicated the channel to be conductive to monovalent cations, which agrees well with our electrophysiology recordings. Moreover, unique structural asymmetry of the SF was revealed by the X-ray structures and MD simulations, implying its importance in ion non-selectivity of tetrameric cation channels. | |||
Asymmetry and ion selectivity properties of bacterial channel NaK mutants derived from ionotropic glutamate receptors.,Minniberger S, Abdolvand S, Braunbeck S, Sun H, Plested AJR J Mol Biol. 2023 Jan 19:167970. doi: 10.1016/j.jmb.2023.167970. PMID:36682679<ref>PMID:36682679</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7pa0" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus cereus ATCC 14579]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Minniberger S]] | [[Category: Minniberger S]] | ||
[[Category: Plested AJR]] | [[Category: Plested AJR]] | ||
Revision as of 15:05, 1 February 2023
NaK C-DI F92A mutant with Rb+ and K+NaK C-DI F92A mutant with Rb+ and K+
Structural highlights
FunctionPublication Abstract from PubMedIonotropic glutamate receptors are ligand-gated cation channels that play essential roles in the excitatory synaptic transmission throughout the central nervous system. A number of open-pore structures of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic-acid (AMPA)-type glutamate receptors became recently available by cryo-electron microscopy (cryo-EM). These structures provide valuable insights into the conformation of the selectivity filter (SF), the part of the ion channel that determines the ion selectivity. Nonetheless, due to the moderate resolution of the cryo-EM structures, detailed information such as ion occupancy of monovalent and divalent cations as well as exact displacement of the side-chains in the SF is still missing. Here, in an attempt to obtain high-resolution information about glutamate receptor SFs, we incorporated partial SF sequences of the AMPA and kainate receptors into the bacterial tetrameric cation channel NaK, which served as a structural scaffold. We determined a series of X-ray structures of NaK-CDI, NaK-SDI and NaK-SELM mutants at 1.42-2.10 A resolution, showing distinct ion occupation of different monovalent cations. Molecular dynamics (MD) simulations of NaK-CDI indicated the channel to be conductive to monovalent cations, which agrees well with our electrophysiology recordings. Moreover, unique structural asymmetry of the SF was revealed by the X-ray structures and MD simulations, implying its importance in ion non-selectivity of tetrameric cation channels. Asymmetry and ion selectivity properties of bacterial channel NaK mutants derived from ionotropic glutamate receptors.,Minniberger S, Abdolvand S, Braunbeck S, Sun H, Plested AJR J Mol Biol. 2023 Jan 19:167970. doi: 10.1016/j.jmb.2023.167970. PMID:36682679[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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