2fy8: Difference between revisions
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<StructureSection load='2fy8' size='340' side='right'caption='[[2fy8]], [[Resolution|resolution]] 2.79Å' scene=''> | <StructureSection load='2fy8' size='340' side='right'caption='[[2fy8]], [[Resolution|resolution]] 2.79Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2fy8]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2fy8]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FY8 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.79Å</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=2fy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fy8 OCA], [https://pdbe.org/2fy8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fy8 RCSB], [https://www.ebi.ac.uk/pdbsum/2fy8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fy8 ProSAT]</span></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=2fy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fy8 OCA], [https://pdbe.org/2fy8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fy8 RCSB], [https://www.ebi.ac.uk/pdbsum/2fy8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fy8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/MTHK_METTH MTHK_METTH] Calcium-gated potassium channel. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Methanothermobacter thermautotrophicus]] | ||
[[Category: | [[Category: Jiang Y]] | ||
[[Category: | [[Category: Ye S]] | ||
Latest revision as of 12:33, 30 August 2023
Crystal structure of MthK rck domain in its ligand-free gating-ring formCrystal structure of MthK rck domain in its ligand-free gating-ring form
Structural highlights
FunctionMTHK_METTH Calcium-gated potassium channel. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMthK is a prokaryotic Ca(2+)-gated K(+) channel that, like other ligand-gated channels, converts the chemical energy of ligand binding to the mechanical force of channel opening. The channel's eight ligand-binding domains, the RCK domains, form an octameric gating ring in which Ca(2+) binding induces conformational changes that open the channel. Here we present the crystal structures of the MthK gating ring in closed and partially open states at 2.8 A, both obtained from the same crystal grown in the absence of Ca(2+). Furthermore, our biochemical and electrophysiological analyses demonstrate that MthK is regulated by both Ca(2+) and pH. Ca(2+) regulates the channel by changing the equilibrium of the gating ring between closed and open states, while pH regulates channel gating by affecting gating-ring stability. Our findings, along with the previously determined open MthK structure, allow us to elucidate the ligand gating mechanism of RCK-regulated K(+) channels. Crystal structures of a ligand-free MthK gating ring: insights into the ligand gating mechanism of K+ channels.,Ye S, Li Y, Chen L, Jiang Y Cell. 2006 Sep 22;126(6):1161-73. PMID:16990139[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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