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5CBG

Calcium activated non-selective cation channel

Summary for 5CBG
Entry DOI10.2210/pdb5cbg/pdb
Related5CBF 5CBH
DescriptorIon transport 2 domain protein, CALCIUM ION, DECYL-BETA-D-MALTOPYRANOSIDE, ... (4 entities in total)
Functional Keywordsmembrane protein, calcium activated non-selective ion channel, 2tm helix ion channel family, tetrameric cation channel, ion transport, transport protein
Biological sourceTsukamurella paurometabola (strain ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040)
Total number of polymer chains6
Total formula weight86478.85
Authors
Dhakshnamoorthy, B.,Rohaim, A.,Rui, H.,Blachowicz, L.,Roux, B. (deposition date: 2015-06-30, release date: 2016-07-20, Last modification date: 2023-09-27)
Primary citationDhakshnamoorthy, B.,Rohaim, A.,Rui, H.,Blachowicz, L.,Roux, B.
Structural and functional characterization of a calcium-activated cation channel from Tsukamurella paurometabola.
Nat Commun, 7:12753-12753, 2016
Cited by
PubMed Abstract: 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 Ca concentration. In the crystal structure, the selectivity filter adopts a novel conformation with Ca 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 Ca 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.
PubMed: 27678077
DOI: 10.1038/ncomms12753
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.14 Å)
Structure validation

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