This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
6vy0
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==SthK P300A cyclic nucleotide-gated potassium channel in a putative active state, in complex with cAMP== | ==SthK P300A cyclic nucleotide-gated potassium channel in a putative active state, in complex with cAMP== | ||
| - | <StructureSection load='6vy0' size='340' side='right'caption='[[6vy0]]' scene=''> | + | <StructureSection load='6vy0' size='340' side='right'caption='[[6vy0]], [[Resolution|resolution]] 6.68Å' 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=6VY0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VY0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6vy0]] 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=6VY0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6VY0 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=6vy0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vy0 OCA], [http://pdbe.org/6vy0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vy0 RCSB], [http://www.ebi.ac.uk/pdbsum/6vy0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vy0 ProSAT]</span></td></tr> | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[6vxz|6vxz]]</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=6vy0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vy0 OCA], [http://pdbe.org/6vy0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6vy0 RCSB], [http://www.ebi.ac.uk/pdbsum/6vy0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6vy0 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 6vy0" 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 06:01, 20 January 2021
SthK P300A cyclic nucleotide-gated potassium channel in a putative active state, in complex with cAMP
| |||||||||||
