5wuc

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Current revision (09:18, 20 March 2024) (edit) (undo)
 
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<StructureSection load='5wuc' size='340' side='right'caption='[[5wuc]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='5wuc' size='340' side='right'caption='[[5wuc]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5wuc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WUC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5WUC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5wuc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WUC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WUC 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=NA:SODIUM+ION'>NA</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]] 1.6&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5wud|5wud]], [[5wue|5wue]], [[5wuf|5wuf]]</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=NA:SODIUM+ION'>NA</scene></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=5wuc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wuc OCA], [http://pdbe.org/5wuc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wuc RCSB], [http://www.ebi.ac.uk/pdbsum/5wuc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wuc ProSAT]</span></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=5wuc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wuc OCA], [https://pdbe.org/5wuc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wuc RCSB], [https://www.ebi.ac.uk/pdbsum/5wuc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wuc 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/Q4J9E6_SULAC Q4J9E6_SULAC]
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Mammalian TRICs function as K+-permeable cation channels that provide counter ions for Ca2+ handling in intracellular stores. Here we describe the structures of two prokaryotic homologues, archaeal SaTRIC and bacterial CpTRIC, showing that TRIC channels are symmetrical trimers with transmembrane pores through each protomer. Each pore holds a string of water molecules centred at kinked helices in two inverted-repeat triple-helix bundles (THBs). The pores are locked in a closed state by a hydrogen bond network at the C terminus of the THBs, which is lost when the pores assume an open conformation. The transition between the open and close states seems to be mediated by cation binding to conserved residues along the three-fold axis. Electrophysiology and mutagenesis studies show that prokaryotic TRICs have similar functional properties to those of mammalian TRICs and implicate the three-fold axis in the allosteric regulation of the channel.
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Structural basis for conductance through TRIC cation channels.,Su M, Gao F, Yuan Q, Mao Y, Li DL, Guo Y, Yang C, Wang XH, Bruni R, Kloss B, Zhao H, Zeng Y, Zhang FB, Marks AR, Hendrickson WA, Chen YH Nat Commun. 2017 May 19;8:15103. doi: 10.1038/ncomms15103. PMID:28524849<ref>PMID:28524849</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 5wuc" 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: Bruni, R]]
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[[Category: Sulfolobus acidocaldarius]]
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[[Category: Chen, Y H]]
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[[Category: Bruni R]]
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[[Category: Gao, F]]
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[[Category: Chen YH]]
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[[Category: Guo, Y Z]]
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[[Category: Gao F]]
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[[Category: Hendrickson, W A]]
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[[Category: Guo YZ]]
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[[Category: Kloss, B]]
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[[Category: Hendrickson WA]]
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[[Category: Li, D L]]
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[[Category: Kloss B]]
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[[Category: Mao, Y]]
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[[Category: Li DL]]
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[[Category: NYCOMPS, New York Consortium on Membrane Protein Structure]]
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[[Category: Mao Y]]
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[[Category: Su, M]]
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[[Category: Su M]]
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[[Category: Wang, X H]]
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[[Category: Wang XH]]
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[[Category: Cation channel]]
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[[Category: Membrane protein]]
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[[Category: New york consortium on membrane protein structure]]
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[[Category: Nycomp]]
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[[Category: Psi-biology]]
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[[Category: Structural genomic]]
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[[Category: Tric]]
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Current revision

Structural basis for conductance through TRIC cation channels

PDB ID 5wuc

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OCA

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