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PDBsum entry 5cbh
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Transport protein
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PDB id
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5cbh
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PDB id:
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| Name: |
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Transport protein
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Title:
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Structural and functional characterization of a calcium-activated cation channel from tsukamurella paurometabola
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Structure:
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Ion transport 2 domain protein. Chain: a, b, c, d, e, f. Engineered: yes
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Source:
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Tsukamurella paurometabola (strain atcc 8368 / dsm 20162 / jcm 10117 / nbrc 16120 / nctc 13040). Organism_taxid: 521096. Strain: atcc 8368 / dsm 20162 / jcm 10117 / nbrc 16120 / nctc 13040. Gene: tpau_1687. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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3.37Å
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R-factor:
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0.234
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R-free:
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0.264
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Authors:
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B.Dhakshnamoorthy,A.Rohaim,H.Rui,L.Blachowicz,B.Roux
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Key ref:
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B.Dhakshnamoorthy
et al.
(2016).
Structural and functional characterization of a calcium-activated cation channel from Tsukamurella paurometabola.
Nat Commun,
7,
12753.
PubMed id:
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Date:
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30-Jun-15
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Release date:
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20-Jul-16
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PROCHECK
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Headers
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References
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D5UM26
(D5UM26_TSUPD) -
Ion transport 2 domain protein from Tsukamurella paurometabola (strain ATCC 8368 / DSM 20162 / CCUG 35730 / CIP 100753 / JCM 10117 / KCTC 9821 / NBRC 16120 / NCIMB 702349 / NCTC 13040)
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Seq:
Struc:
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123 a.a.
102 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Nat Commun
7:12753
(2016)
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PubMed id:
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Structural and functional characterization of a calcium-activated cation channel from Tsukamurella paurometabola.
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B.Dhakshnamoorthy,
A.Rohaim,
H.Rui,
L.Blachowicz,
B.Roux.
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ABSTRACT
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The selectivity filter is an essential functional element of
K+channels that is highly conserved both in terms of its primary
sequence and its three-dimensional structure. Here, we investigate the
properties of an ion channel from the Gram-positive bacterium Tsukamurella
paurometabola with a selectivity filter formed by an uncommon proline-rich
sequence. Electrophysiological recordings show that it is a non-selective cation
channel and that its activity depends on Ca2+concentration. In the
crystal structure, the selectivity filter adopts a novel conformation with
Ca2+ions bound within the filter near the pore helix where they are
coordinated by backbone oxygen atoms, a recurrent motif found in multiple
proteins. The binding of Ca2+ion in the selectivity filter controls
the widening of the pore as shown in crystal structures and in molecular
dynamics simulations. The structural, functional and computational data provide
a characterization of this calcium-gated cationic channel.
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Links
