8srb: Difference between revisions
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==Cryo-EM structure of TRPM2 chanzyme in the presence of EDTA and ADP-ribose== | |||
<StructureSection load='8srb' size='340' side='right'caption='[[8srb]], [[Resolution|resolution]] 2.82Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8srb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Salpingoeca_rosetta Salpingoeca rosetta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8SRB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8SRB FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.82Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=APR:ADENOSINE-5-DIPHOSPHORIBOSE'>APR</scene>, <scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene></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=8srb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8srb OCA], [https://pdbe.org/8srb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8srb RCSB], [https://www.ebi.ac.uk/pdbsum/8srb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8srb ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/F2UB89_SALR5 F2UB89_SALR5] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Channel enzymes represent a class of ion channels with enzymatic activity directly or indirectly linked to their channel function. We investigated a TRPM2 chanzyme from choanoflagellates that integrates two seemingly incompatible functions into a single peptide: a channel module activated by ADP-ribose with high open probability and an enzyme module (NUDT9-H domain) consuming ADP-ribose at a remarkably slow rate. Using time-resolved cryogenic-electron microscopy, we captured a complete series of structural snapshots of gating and catalytic cycles, revealing the coupling mechanism between channel gating and enzymatic activity. The slow kinetics of the NUDT9-H enzyme module confers a self-regulatory mechanism: ADPR binding triggers NUDT9-H tetramerization, promoting channel opening, while subsequent hydrolysis reduces local ADPR, inducing channel closure. We further demonstrated how the NUDT9-H domain has evolved from a structurally semi-independent ADP-ribose hydrolase module in early species to a fully integrated component of a gating ring essential for channel activation in advanced species. | |||
Coupling enzymatic activity and gating in an ancient TRPM chanzyme and its molecular evolution.,Huang Y, Kumar S, Lee J, Lu W, Du J Nat Struct Mol Biol. 2024 May 21. doi: 10.1038/s41594-024-01316-4. PMID:38773335<ref>PMID:38773335</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8srb" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Salpingoeca rosetta]] | |||
[[Category: Du J]] | |||
[[Category: Huang Y]] | |||
[[Category: Kumar S]] | |||
[[Category: Lu W]] | |||
Latest revision as of 08:59, 5 June 2024
Cryo-EM structure of TRPM2 chanzyme in the presence of EDTA and ADP-riboseCryo-EM structure of TRPM2 chanzyme in the presence of EDTA and ADP-ribose
Structural highlights
FunctionPublication Abstract from PubMedChannel enzymes represent a class of ion channels with enzymatic activity directly or indirectly linked to their channel function. We investigated a TRPM2 chanzyme from choanoflagellates that integrates two seemingly incompatible functions into a single peptide: a channel module activated by ADP-ribose with high open probability and an enzyme module (NUDT9-H domain) consuming ADP-ribose at a remarkably slow rate. Using time-resolved cryogenic-electron microscopy, we captured a complete series of structural snapshots of gating and catalytic cycles, revealing the coupling mechanism between channel gating and enzymatic activity. The slow kinetics of the NUDT9-H enzyme module confers a self-regulatory mechanism: ADPR binding triggers NUDT9-H tetramerization, promoting channel opening, while subsequent hydrolysis reduces local ADPR, inducing channel closure. We further demonstrated how the NUDT9-H domain has evolved from a structurally semi-independent ADP-ribose hydrolase module in early species to a fully integrated component of a gating ring essential for channel activation in advanced species. Coupling enzymatic activity and gating in an ancient TRPM chanzyme and its molecular evolution.,Huang Y, Kumar S, Lee J, Lu W, Du J Nat Struct Mol Biol. 2024 May 21. doi: 10.1038/s41594-024-01316-4. PMID:38773335[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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