5CBH

Structural and Functional Characterization of a Calcium-activated Cation channel from Tsukamurella Paurometabola

5CBH の概要

• エントリーDOI: 10.2210/pdb5cbh/pdb
• 関連するPDBエントリー: 5CBF 5CBG
• 分子名称: Ion transport 2 domain protein, CALCIUM ION (3 entities in total)
• 機能のキーワード: membrane protein, calcium activated non-selective ion channel, 2tm helix ion channel family, tetrameric cation channel, ion transport, transport protein
• 由来する生物種: Tsukamurella paurometabola (strain ATCC 8368 / DSM 20162 / JCM 10117 / NBRC 16120 / NCTC 13040)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 85031.17

構造登録者

Dhakshnamoorthy, B.,Rohaim, A.,Rui, H.,Blachowicz, L.,Roux, B. (登録日: 2015-06-30, 公開日: 2016-07-20, 最終更新日: 2023-09-27)

主引用文献

Dhakshnamoorthy, 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

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

実験手法

X-RAY DIFFRACTION (3.37 Å)