5EIK

Structure of a Trimeric Intracellular Cation channel from C. elegans in the absence of Ca2+

5EIK の概要

• エントリーDOI: 10.2210/pdb5eik/pdb
• 関連するPDBエントリー: 5EGI
• 分子名称: Uncharacterized protein Y57A10A.28, [(2R)-1-octadecanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phospho ryl]oxy-propan-2-yl] (8Z)-icosa-5,8,11,14-tetraenoate, 1-PALMITOYL-2-LINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE, ... (7 entities in total)
• 機能のキーワード: membrane protein, cation channel
• 由来する生物種: Caenorhabditis elegans
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33206.07

構造登録者

Hu, M.H.,Yang, H.T.,Liu, Z.F. (登録日: 2015-10-30, 公開日: 2016-10-05, 最終更新日: 2023-11-08)

主引用文献

Yang, H.T.,Hu, M.H.,Guo, J.L.,Ou, X.M.,Cai, T.X.,Liu, Z.F.
Pore architecture of TRIC channels and insights into their gating mechanism.
Nature, 538:537-541, 2016

PubMed Abstract: Intracellular Ca signalling processes are fundamental to muscle contraction, neurotransmitter release, cell growth and apoptosis. Release of Ca from the intracellular stores is supported by a series of ion channels in sarcoplasmic or endoplasmic reticulum (SR/ER). Among them, two isoforms of the trimeric intracellular cation (TRIC) channel family, named TRIC-A and TRIC-B, modulate the release of Ca through the ryanodine receptor or inositol triphosphate receptor, and maintain the homeostasis of ions within SR/ER lumen. Genetic ablations or mutations of TRIC channels are associated with hypertension, heart disease, respiratory defects and brittle bone disease. Despite the pivotal function of TRIC channels in Ca signalling, their pore architectures and gating mechanisms remain unknown. Here we present the structures of TRIC-B1 and TRIC-B2 channels from Caenorhabditis elegans in complex with endogenous phosphatidylinositol-4,5-biphosphate (PtdIns(4,5)P, also known as PIP) lipid molecules. The TRIC-B1/B2 proteins and PIP assemble into a symmetrical homotrimeric complex. Each monomer contains an hourglass-shaped hydrophilic pore contained within a seven-transmembrane-helix domain. Structural and functional analyses unravel the central role of PIP in stabilizing the cytoplasmic gate of the ion permeation pathway and reveal a marked Ca-induced conformational change in a cytoplasmic loop above the gate. A mechanistic model has been proposed to account for the complex gating mechanism of TRIC channels.

PubMed: 27698420
DOI: 10.1038/nature19767

実験手法

X-RAY DIFFRACTION (2.3 Å)