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PDBsum entry 5cbh

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Transport protein PDB id
5cbh
Contents
Protein chains
(+ 0 more) 102 a.a.
Metals
_CA ×8
Waters ×1

References listed in PDB file
Key reference
Title Structural and functional characterization of a calcium-Activated cation channel from tsukamurella paurometabola.
Authors B.Dhakshnamoorthy, A.Rohaim, H.Rui, L.Blachowicz, B.Roux.
Ref. Nat Commun, 2016, 7, 12753.
PubMed id 27678077
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 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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 Headers

 

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