3vvi

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<StructureSection load='3vvi' size='340' side='right'caption='[[3vvi]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
<StructureSection load='3vvi' size='340' side='right'caption='[[3vvi]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3vvi]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VVI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3vvi]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Fusarium_graminearum_PH-1 Fusarium graminearum PH-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VVI 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=ACT:ACETATE+ION'>ACT</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">X-ray diffraction, [[Resolution|Resolution]] 1.25&#8491;</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=ACT:ACETATE+ION'>ACT</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=3vvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vvi OCA], [https://pdbe.org/3vvi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vvi RCSB], [https://www.ebi.ac.uk/pdbsum/3vvi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vvi ProSAT]</span></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=3vvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vvi OCA], [https://pdbe.org/3vvi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vvi RCSB], [https://www.ebi.ac.uk/pdbsum/3vvi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vvi ProSAT]</span></td></tr>
</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/I1RJZ4_GIBZE I1RJZ4_GIBZE]
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Multimodal activation by various stimuli is a fundamental characteristic of TRP channels. We identified a fungal TRP channel, TRPGz, exhibiting activation by hyperosmolarity, temperature increase, cytosolic Ca(2+) elevation, membrane potential, and H2O2 application, and thus it is expected to represent a prototypic multimodal TRP channel. TRPGz possesses a cytosolic C-terminal domain (CTD), primarily composed of intrinsically disordered regions with some regulatory modules, a putative coiled-coil region and a basic residue cluster. The CTD oligomerization mediated by the coiled-coil region is required for the hyperosmotic and temperature increase activations but not for the tetrameric channel formation or other activation modalities. In contrast, the basic cluster is responsible for general channel inhibition, by binding to phosphatidylinositol phosphates. The crystal structure of the presumed coiled-coil region revealed a tetrameric assembly in an offset spiral rather than a canonical coiled-coil. This structure underlies the observed moderate oligomerization affinity enabling the dynamic assembly and disassembly of the CTD during channel functions, which are compatible with the multimodal regulation mediated by each functional module.
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Molecular bases of multimodal regulation of a fungal transient receptor potential (TRP) channel.,Ihara M, Hamamoto S, Miyanoiri Y, Takeda M, Kainosho M, Yabe I, Uozumi N, Yamashita A J Biol Chem. 2013 May 24;288(21):15303-17. doi: 10.1074/jbc.M112.434795. Epub, 2013 Apr 3. PMID:23553631<ref>PMID:23553631</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 3vvi" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Fusarium graminearum PH-1]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Ihara, M]]
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[[Category: Ihara M]]
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[[Category: Yamashita, A]]
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[[Category: Yamashita A]]
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[[Category: Coiled-coil]]
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[[Category: Ion channel]]
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[[Category: Osomosensor]]
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[[Category: Regulation of the channel function]]
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[[Category: Transport protein]]
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Current revision

Crystal structure of the coiled-coil domain of the transient receptor potential channel from Gibberella zeae (TRPGz)

PDB ID 3vvi

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