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6pkv

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==Cryo-EM structure of the zebrafish TRPM2 channel in the apo conformation, processed with C4 symmetry==
==Cryo-EM structure of the zebrafish TRPM2 channel in the apo conformation, processed with C4 symmetry==
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<StructureSection load='6pkv' size='340' side='right'caption='[[6pkv]], [[Resolution|resolution]] 4.30&Aring;' scene=''>
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<SX load='6pkv' size='340' side='right' viewer='molstar' caption='[[6pkv]], [[Resolution|resolution]] 4.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6pkv]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Brachidanio_rerio Brachidanio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PKV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6PKV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6pkv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6PKV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6PKV FirstGlance]. <br>
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</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</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]] 4.3&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">trpm2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7955 Brachidanio rerio])</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=6pkv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pkv OCA], [https://pdbe.org/6pkv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6pkv RCSB], [https://www.ebi.ac.uk/pdbsum/6pkv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6pkv 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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6pkv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6pkv OCA], [http://pdbe.org/6pkv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6pkv RCSB], [http://www.ebi.ac.uk/pdbsum/6pkv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6pkv 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/TRPM2_DANRE TRPM2_DANRE] Nonselective, voltage-independent cation channel that mediates Ca(2+) influx, leading to increased cytoplasmic Ca(2+) levels. Functions as ligand-gated ion channel. Binding of ADP-ribose to the cytoplasmic N-terminal region causes a conformation change; the channel is primed but still requires Ca(2+) binding to trigger channel opening.<ref>PMID:30250252</ref>
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The transient receptor potential melastatin 2 (TRPM2) channel plays a key role in redox sensation in many cell types. Channel activation requires binding of both ADP-ribose (ADPR) and Ca(2+). The recently published TRPM2 structures from Danio rerio in the ligand-free and the ADPR/Ca(2+)-bound conditions represent the channel in closed and open states, which uncovered substantial tertiary and quaternary conformational rearrangements. However, it is unclear how these rearrangements are achieved within the tetrameric channel during channel gating. Here we report the cryo-electron microscopy structures of Danio rerio TRPM2 in the absence of ligands, in complex with Ca(2+) alone, and with both ADPR and Ca(2+), resolved to ~4.3 A, ~3.8 A, and ~4.2 A, respectively. In contrast to the published results, our studies capture ligand-bound TRPM2 structures in two-fold symmetric intermediate states, offering a glimpse of the structural transitions that bridge the closed and open conformations.
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Visualizing structural transitions of ligand-dependent gating of the TRPM2 channel.,Yin Y, Wu M, Hsu AL, Borschel WF, Borgnia MJ, Lander GC, Lee SY Nat Commun. 2019 Aug 20;10(1):3740. doi: 10.1038/s41467-019-11733-5. PMID:31431622<ref>PMID:31431622</ref>
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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 6pkv" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
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</StructureSection>
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</SX>
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[[Category: Brachidanio rerio]]
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[[Category: Danio rerio]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Borgnia, M J]]
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[[Category: Borgnia MJ]]
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[[Category: Borschel, W F]]
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[[Category: Borschel WF]]
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[[Category: Hsu, A L]]
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[[Category: Hsu AL]]
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[[Category: Lander, G C]]
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[[Category: Lander GC]]
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[[Category: Lee, S Y]]
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[[Category: Lee S-Y]]
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[[Category: Wu, M]]
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[[Category: Wu M]]
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[[Category: Yin, Y]]
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[[Category: Yin Y]]
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[[Category: Adp-ribose]]
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[[Category: Calcium-permeable ion channel]]
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[[Category: Ion channel]]
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[[Category: Redox sensor]]
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[[Category: Transport protein]]
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[[Category: Trp channel]]
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[[Category: Trpm channel]]
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[[Category: Warmth sensor]]
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Current revision

Cryo-EM structure of the zebrafish TRPM2 channel in the apo conformation, processed with C4 symmetry

6pkv, resolution 4.30Å

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