6whg
From Proteopedia
(Difference between revisions)
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==PI3P and calcium bound full-length TRPY1 in detergent== | ==PI3P and calcium bound full-length TRPY1 in detergent== | ||
| - | <StructureSection load='6whg' size='340' side='right'caption='[[6whg]]' scene=''> | + | <StructureSection load='6whg' size='340' side='right'caption='[[6whg]], [[Resolution|resolution]] 3.10Å' 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=6WHG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WHG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6whg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WHG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WHG FirstGlance]. <br> |
| - | </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=6whg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6whg OCA], [https://pdbe.org/6whg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6whg RCSB], [https://www.ebi.ac.uk/pdbsum/6whg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6whg 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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PWE:(2R)-1-(butanoyloxy)-3-{[(R)-hydroxy{[(1S,2S,3S,4S,5S,6R)-2,3,4,6-tetrahydroxy-5-(phosphonooxy)cyclohexyl]oxy}phosphoryl]oxy}propan-2-yl+hexadecanoate'>PWE</scene></td></tr> |
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YVC1, YOR087W, YOR088W, YOR3151W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=6whg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6whg OCA], [https://pdbe.org/6whg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6whg RCSB], [https://www.ebi.ac.uk/pdbsum/6whg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6whg ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/YVC1_YEAST YVC1_YEAST]] Required for release of calcium ions from the vacuole in response to hyperosmotic shock.<ref>PMID:11427713</ref> <ref>PMID:11781332</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Transient receptor potential (TRP) channels emerged in fungi as mechanosensitive osmoregulators. The Saccharomyces cerevisiae vacuolar TRP yeast 1 (TRPY1) is the most studied TRP channel from fungi, but the structure and details of channel modulation remain elusive. Here, we describe the full-length cryoelectron microscopy structure of TRPY1 at 3.1 A resolution in a closed state. The structure, despite containing an evolutionarily conserved and archetypical transmembrane domain, reveals distinctive structural folds for the cytosolic N and C termini, compared with other eukaryotic TRP channels. We identify an inhibitory phosphatidylinositol 3-phosphate (PI(3)P) lipid-binding site, along with two Ca(2+)-binding sites: a cytosolic site, implicated in channel activation and a vacuolar lumen site, implicated in inhibition. These findings, together with data from microsecond-long molecular dynamics simulations and a model of a TRPY1 open state, provide insights into the basis of TRPY1 channel modulation by lipids and Ca(2+), and the molecular evolution of TRP channels. | ||
| + | |||
| + | Structure of the ancient TRPY1 channel from Saccharomyces cerevisiae reveals mechanisms of modulation by lipids and calcium.,Ahmed T, Nisler CR, Fluck EC 3rd, Walujkar S, Sotomayor M, Moiseenkova-Bell VY Structure. 2021 Aug 24. pii: S0969-2126(21)00298-7. doi:, 10.1016/j.str.2021.08.003. PMID:34453887<ref>PMID:34453887</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6whg" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Atcc 18824]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Ahmed T]] | + | [[Category: Ahmed, T]] |
| - | [[Category: Moiseenkova-Bell | + | [[Category: Moiseenkova-Bell, V Y]] |
| + | [[Category: Ion channel]] | ||
| + | [[Category: Membrane protein]] | ||
Revision as of 15:54, 3 November 2021
PI3P and calcium bound full-length TRPY1 in detergent
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