|
|
| Line 3: |
Line 3: |
| | <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 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> | + | <table><tr><td colspan='2'>[[5e1j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. 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 [https://proteopedia.org/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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.308Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5e1j 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=5e1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5e1j OCA], [https://pdbe.org/5e1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5e1j RCSB], [https://www.ebi.ac.uk/pdbsum/5e1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5e1j ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TPC1_ARATH 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.<ref>PMID:15464979</ref> <ref>PMID:15772667</ref> | + | [https://www.uniprot.org/uniprot/TPC1_ARATH 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.<ref>PMID:15464979</ref> <ref>PMID:15772667</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 26: |
Line 26: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, L]] | + | [[Category: Chen L]] |
| - | [[Category: Chen, Q]] | + | [[Category: Chen Q]] |
| - | [[Category: Guo, J]] | + | [[Category: Guo J]] |
| - | [[Category: Jiang, Y]] | + | [[Category: Jiang Y]] |
| - | [[Category: Lee, C]] | + | [[Category: Lee C]] |
| - | [[Category: Yang, Y]] | + | [[Category: Yang Y]] |
| - | [[Category: Zeng, W]] | + | [[Category: Zeng W]] |
| - | [[Category: Calcium modulation]]
| + | |
| - | [[Category: Metal transport]]
| + | |
| - | [[Category: Two-pore channel]]
| + | |
| - | [[Category: Voltage-gated]]
| + | |
| 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 PubMed
Two-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.
See Also
References
- ↑ Kawano T, Kadono T, Fumoto K, Lapeyrie F, Kuse M, Isobe M, Furuichi T, Muto S. Aluminum as a specific inhibitor of plant TPC1 Ca2+ channels. Biochem Biophys Res Commun. 2004 Nov 5;324(1):40-5. PMID:15464979 doi:http://dx.doi.org/S0006-291X(04)02051-0
- ↑ Peiter E, Maathuis FJ, Mills LN, Knight H, Pelloux J, Hetherington AM, Sanders D. The vacuolar Ca2+-activated channel TPC1 regulates germination and stomatal movement. Nature. 2005 Mar 17;434(7031):404-8. PMID:15772667 doi:http://dx.doi.org/nature03381
- ↑ Guo J, Zeng W, Chen Q, Lee C, Chen L, Yang Y, Cang C, Ren D, Jiang Y. Structure of the voltage-gated two-pore channel TPC1 from Arabidopsis thaliana. Nature. 2015 Dec 21. doi: 10.1038/nature16446. PMID:26689363 doi:http://dx.doi.org/10.1038/nature16446
|
