5e1j: Difference between revisions
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<StructureSection load='5e1j' size='340' side='right' caption='[[5e1j]], [[Resolution|resolution]] 3.31Å' scene=''> | <StructureSection load='5e1j' size='340' side='right' caption='[[5e1j]], [[Resolution|resolution]] 3.31Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5e1j]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E1J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E1J FirstGlance]. <br> | <table><tr><td colspan='2'>[[5e1j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5E1J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5E1J FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BA:BARIUM+ION'>BA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BA:BARIUM+ION'>BA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
<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=5e1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e1j OCA], [http://pdbe.org/5e1j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e1j RCSB], [http://www.ebi.ac.uk/pdbsum/5e1j PDBsum]</span></td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TPC1, CCH1, FOU2, At4g03560, F9H3.19, T5L23.5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | ||
<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=5e1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e1j OCA], [http://pdbe.org/5e1j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5e1j RCSB], [http://www.ebi.ac.uk/pdbsum/5e1j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e1j ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Arath]] | |||
[[Category: Chen, L]] | [[Category: Chen, L]] | ||
[[Category: Chen, Q]] | [[Category: Chen, Q]] | ||
Revision as of 12:53, 22 November 2017
Structure of voltage-gated two-pore channel TPC1 from Arabidopsis thalianaStructure of voltage-gated two-pore channel TPC1 from Arabidopsis thaliana
Structural highlights
Function[TPC1_ARATH] Functions as a voltage-gated inward-rectifying Ca(2+) channel (VDCC) across the vacuole membrane. Is one of the essential components of the slow vacuolar (SV) channel. Acts as the major ROS-responsive Ca(2+) channel and is the possible target of Al-dependent inhibition. Involved in the regulation of germination and stomatal movement.[1] [2] Publication Abstract from PubMedTwo-pore channels (TPCs) contain two copies of a Shaker-like six-transmembrane (6-TM) domain in each subunit and are ubiquitously expressed in both animals and plants as organellar cation channels. Here we present the crystal structure of a vacuolar two-pore channel from Arabidopsis thaliana, AtTPC1, which functions as a homodimer. AtTPC1 activation requires both voltage and cytosolic Ca2+. Ca2+ binding to the cytosolic EF-hand domain triggers conformational changes coupled to the pair of pore-lining inner helices from the first 6-TM domains, whereas membrane potential only activates the second voltage-sensing domain, the conformational changes of which are coupled to the pair of inner helices from the second 6-TM domains. Luminal Ca2+ or Ba2+ can modulate voltage activation by stabilizing the second voltage-sensing domain in the resting state and shift voltage activation towards more positive potentials. Our Ba2+-bound AtTPC1 structure reveals a voltage sensor in the resting state, providing hitherto unseen structural insight into the general voltage-gating mechanism among voltage-gated channels. Structure of the voltage-gated two-pore channel TPC1 from Arabidopsis thaliana.,Guo J, Zeng W, Chen Q, Lee C, Chen L, Yang Y, Cang C, Ren D, Jiang Y Nature. 2015 Dec 21. doi: 10.1038/nature16446. PMID:26689363[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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