6vxz

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Current revision (14:40, 6 March 2024) (edit) (undo)
 
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<StructureSection load='6vxz' size='340' side='right'caption='[[6vxz]], [[Resolution|resolution]] 3.42&Aring;' scene=''>
<StructureSection load='6vxz' size='340' side='right'caption='[[6vxz]], [[Resolution|resolution]] 3.42&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<table><tr><td colspan='2'>[[6vxz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Spirochaeta_thermophila_DSM_6578 Spirochaeta thermophila DSM 6578]. 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 [https://proteopedia.org/fgij/fg.htm?mol=6VXZ FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.42&#8491;</td></tr>
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<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>
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<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>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6vxz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6vxz OCA], [https://pdbe.org/6vxz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6vxz RCSB], [https://www.ebi.ac.uk/pdbsum/6vxz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6vxz ProSAT]</span></td></tr>
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<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>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/G0GA88_SPITZ G0GA88_SPITZ]
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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.
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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>
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==See Also==
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*[[Ion channels 3D structures|Ion channels 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6vxz" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Spitz]]
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[[Category: Spirochaeta thermophila DSM 6578]]
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[[Category: Nimigean, C M]]
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[[Category: Nimigean CM]]
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[[Category: Rheinberger, J]]
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[[Category: Rheinberger J]]
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[[Category: Schmidpeter, P A.M]]
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[[Category: Schmidpeter PAM]]
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[[Category: Transport protein]]
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Current revision

SthK P300A cyclic nucleotide-gated potassium channel in the closed state, in complex with cAMP

PDB ID 6vxz

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