6vxz
From Proteopedia
(Difference between revisions)
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==SthK P300A cyclic nucleotide-gated potassium channel in the closed state, in complex with cAMP== | ==SthK P300A cyclic nucleotide-gated potassium channel in the closed state, in complex with cAMP== | ||
| - | <StructureSection load='6vxz' size='340' side='right'caption='[[6vxz]]' scene=''> | + | <StructureSection load='6vxz' size='340' side='right'caption='[[6vxz]], [[Resolution|resolution]] 3.42Å' 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=6VXZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VXZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6vxz]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Spitz Spitz]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6VXZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VXZ FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6vxz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vxz OCA], [http://pdbe.org/6vxz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vxz RCSB], [http://www.ebi.ac.uk/pdbsum/6vxz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vxz 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=CMP:ADENOSINE-3,5-CYCLIC-MONOPHOSPHATE'>CMP</scene>, <scene name='pdbligand=PGW:(1R)-2-{[(S)-{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(HEXADECANOYLOXY)METHYL]ETHYL+(9Z)-OCTADEC-9-ENOATE'>PGW</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6cju|6cju]], [[6vy0|6vy0]]</div></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Spith_0644 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=869211 SPITZ])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6vxz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vxz OCA], [http://pdbe.org/6vxz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vxz RCSB], [http://www.ebi.ac.uk/pdbsum/6vxz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vxz ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | SthK, a cyclic nucleotide-modulated ion channel from Spirochaeta thermophila, activates slowly upon cAMP increase. This is reminiscent of the slow, cAMP-induced activation reported for the hyperpolarization-activated and cyclic nucleotide-gated channel HCN2 in the family of so-called pacemaker channels. Here, we investigate slow cAMP-induced activation in purified SthK channels using stopped-flow assays, mutagenesis, enzymatic catalysis and inhibition assays revealing that the cis/trans conformation of a conserved proline in the cyclic nucleotide-binding domain determines the activation kinetics of SthK. We propose that SthK exists in two forms: trans Pro300 SthK with high ligand binding affinity and fast activation, and cis Pro300 SthK with low affinity and slow activation. Following channel activation, the cis/trans equilibrium, catalyzed by prolyl isomerases, is shifted towards trans, while steady-state channel activity is unaffected. Our results reveal prolyl isomerization as a regulatory mechanism for SthK, and potentially eukaryotic HCN channels. This mechanism could contribute to electrical rhythmicity in cells. | ||
| + | |||
| + | Prolyl isomerization controls activation kinetics of a cyclic nucleotide-gated ion channel.,Schmidpeter PAM, Rheinberger J, Nimigean CM Nat Commun. 2020 Dec 16;11(1):6401. doi: 10.1038/s41467-020-20104-4. PMID:33328472<ref>PMID:33328472</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6vxz" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Nimigean | + | [[Category: Spitz]] |
| - | [[Category: Rheinberger J]] | + | [[Category: Nimigean, C M]] |
| - | [[Category: Schmidpeter | + | [[Category: Rheinberger, J]] |
| + | [[Category: Schmidpeter, P A.M]] | ||
| + | [[Category: Transport protein]] | ||
Revision as of 06:00, 20 January 2021
SthK P300A cyclic nucleotide-gated potassium channel in the closed state, in complex with cAMP
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