6WHG

PI3P and calcium bound full-length TRPY1 in detergent

6WHG の概要

• エントリーDOI: 10.2210/pdb6whg/pdb
• EMDBエントリー: 21672
• 分子名称: Calcium channel YVC1, CALCIUM ION, (2R)-1-(butanoyloxy)-3-{[(R)-hydroxy{[(1S,2S,3S,4S,5S,6R)-2,3,4,6-tetrahydroxy-5-(phosphonooxy)cyclohexyl]oxy}phosphoryl]oxy}propan-2-yl hexadecanoate (3 entities in total)
• 機能のキーワード: ion channel, membrane protein
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 315349.80

構造登録者

Ahmed, T.,Moiseenkova-Bell, V.Y. (登録日: 2020-04-08, 公開日: 2021-04-21, 最終更新日: 2024-05-29)

主引用文献

Ahmed, T.,Nisler, C.R.,Fluck 3rd, E.C.,Walujkar, S.,Sotomayor, M.,Moiseenkova-Bell, V.Y.
Structure of the ancient TRPY1 channel from Saccharomyces cerevisiae reveals mechanisms of modulation by lipids and calcium.
Structure, 30:139-, 2022

PubMed Abstract: Transient receptor potential (TRP) channels emerged in fungi as mechanosensitive osmoregulators. The Saccharomyces cerevisiae vacuolar TRP yeast 1 (TRPY1) is the most studied TRP channel from fungi, but the structure and details of channel modulation remain elusive. Here, we describe the full-length cryoelectron microscopy structure of TRPY1 at 3.1 Å resolution in a closed state. The structure, despite containing an evolutionarily conserved and archetypical transmembrane domain, reveals distinctive structural folds for the cytosolic N and C termini, compared with other eukaryotic TRP channels. We identify an inhibitory phosphatidylinositol 3-phosphate (PI(3)P) lipid-binding site, along with two Ca-binding sites: a cytosolic site, implicated in channel activation and a vacuolar lumen site, implicated in inhibition. These findings, together with data from microsecond-long molecular dynamics simulations and a model of a TRPY1 open state, provide insights into the basis of TRPY1 channel modulation by lipids and Ca, and the molecular evolution of TRP channels.

PubMed: 34453887
DOI: 10.1016/j.str.2021.08.003

実験手法

ELECTRON MICROSCOPY (3.1 Å)