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PDBsum entry 5e1j
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Metal transport
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PDB id
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5e1j
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PDB id:
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| Name: |
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Metal transport
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Title:
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Structure of voltage-gated two-pore channel tpc1 from arabidopsis thaliana
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Structure:
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Two pore calcium channel protein 1. Chain: a. Synonym: calcium channel protein 1,atcch1,fatty acid oxygenation up- regulated protein 2,voltage-dependent calcium channel protein tpc1, attpc1. Engineered: yes
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Source:
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Arabidopsis thaliana. Mouse-ear cress. Organism_taxid: 3702. Gene: tpc1, cch1, fou2, at4g03560, f9h3.19, t5l23.5. Expressed in: komagataella pastoris. Expression_system_taxid: 4922.
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Resolution:
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3.31Å
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R-factor:
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0.325
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R-free:
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0.332
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Authors:
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J.Guo,W.Zeng,Q.Chen,C.Lee,L.Chen,Y.Yang,Y.Jiang
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Key ref:
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J.Guo
et al.
(2016).
Structure of the voltage-gated two-pore channel TPC1 from Arabidopsis thaliana.
Nature,
531,
196-201.
PubMed id:
DOI:
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Date:
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29-Sep-15
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Release date:
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16-Dec-15
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PROCHECK
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Headers
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References
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Q94KI8
(TPC1_ARATH) -
Two pore calcium channel protein 1 from Arabidopsis thaliana
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Seq:
Struc:
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733 a.a.
616 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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DOI no:
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Nature
531:196-201
(2016)
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PubMed id:
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Structure of the voltage-gated two-pore channel TPC1 from Arabidopsis thaliana.
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J.Guo,
W.Zeng,
Q.Chen,
C.Lee,
L.Chen,
Y.Yang,
C.Cang,
D.Ren,
Y.Jiang.
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ABSTRACT
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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 Ca(2+).
Ca(2+) 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 Ca(2+) or Ba(2+) can modulate voltage
activation by stabilizing the second voltage-sensing domain in the resting state
and shift voltage activation towards more positive potentials. Our Ba(2+)-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.
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