4h33: Difference between revisions
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The | ==Crystal structure of a voltage-gated K+ channel pore module in a closed state in lipid membranes, tetragonal crystal form== | ||
<StructureSection load='4h33' size='340' side='right'caption='[[4h33]], [[Resolution|resolution]] 3.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4h33]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes_EGD-e Listeria monocytogenes EGD-e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4H33 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4H33 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]] 3.1Å</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=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</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=4h33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4h33 OCA], [https://pdbe.org/4h33 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4h33 RCSB], [https://www.ebi.ac.uk/pdbsum/4h33 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4h33 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8Y5K1_LISMO Q8Y5K1_LISMO] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Voltage-gated K(+) channels underlie the electrical excitability of cells. Each subunit of the functional tetramer consists of the tandem fusion of two modules, an N-terminal voltage-sensor and a C-terminal pore. To investigate how sensor coupling to the pore generates voltage-dependent channel opening, we solved the crystal structure and characterized the function of a voltage-gated K(+) channel pore in a lipid membrane. The structure of a functional channel in a membrane environment at 3.1 A resolution establishes an unprecedented connection between channel structure and function. The structure is unique in delineating an ion-occupied ready to conduct selectivity filter, a confined aqueous cavity, and a closed activation gate, embodying a dynamic entity trapped in an unstable closed state. | |||
Crystal Structure of a Voltage-gated K+ Channel Pore Module in a Closed State in Lipid Membranes.,Santos JS, Asmar-Rovira GA, Han GW, Liu W, Syeda R, Cherezov V, Baker KA, Stevens RC, Montal M J Biol Chem. 2012 Dec 14;287(51):43063-70. doi: 10.1074/jbc.M112.415091. Epub, 2012 Oct 24. PMID:23095758<ref>PMID:23095758</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4h33" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Listeria monocytogenes EGD-e]] | |||
[[Category: Asmar-Rovira GA]] | |||
[[Category: Baker KA]] | |||
[[Category: Cherezov V]] | |||
[[Category: Han GW]] | |||
[[Category: Liu W]] | |||
[[Category: Montal M]] | |||
[[Category: Santos JS]] | |||
[[Category: Stevens RC]] | |||
[[Category: Syeda R]] | |||
Latest revision as of 17:59, 20 September 2023
Crystal structure of a voltage-gated K+ channel pore module in a closed state in lipid membranes, tetragonal crystal formCrystal structure of a voltage-gated K+ channel pore module in a closed state in lipid membranes, tetragonal crystal form
Structural highlights
FunctionPublication Abstract from PubMedVoltage-gated K(+) channels underlie the electrical excitability of cells. Each subunit of the functional tetramer consists of the tandem fusion of two modules, an N-terminal voltage-sensor and a C-terminal pore. To investigate how sensor coupling to the pore generates voltage-dependent channel opening, we solved the crystal structure and characterized the function of a voltage-gated K(+) channel pore in a lipid membrane. The structure of a functional channel in a membrane environment at 3.1 A resolution establishes an unprecedented connection between channel structure and function. The structure is unique in delineating an ion-occupied ready to conduct selectivity filter, a confined aqueous cavity, and a closed activation gate, embodying a dynamic entity trapped in an unstable closed state. Crystal Structure of a Voltage-gated K+ Channel Pore Module in a Closed State in Lipid Membranes.,Santos JS, Asmar-Rovira GA, Han GW, Liu W, Syeda R, Cherezov V, Baker KA, Stevens RC, Montal M J Biol Chem. 2012 Dec 14;287(51):43063-70. doi: 10.1074/jbc.M112.415091. Epub, 2012 Oct 24. PMID:23095758[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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