- EMDB-31587: Structure of AtTPC1 D240A/D454A/E528A mutant with 1 mM Ca2+ -
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基本情報
登録情報
データベース: EMDB / ID: EMD-31587
タイトル
Structure of AtTPC1 D240A/D454A/E528A mutant with 1 mM Ca2+
マップデータ
Structure of AtTPC1 D240A/D454A/E528A mutant with 1 mM Ca2
試料
複合体: AtTPC1 D240A/D454A/E528A mutant homodimer
タンパク質・ペプチド: Two pore calcium channel protein 1,GFP
リガンド: CALCIUM ION
機能・相同性
機能・相同性情報
regulation of jasmonic acid biosynthetic process / seed germination / regulation of stomatal movement / plant-type vacuole / vacuole / vacuolar membrane / monoatomic ion channel complex / voltage-gated calcium channel activity / bioluminescence / generation of precursor metabolites and energy ...regulation of jasmonic acid biosynthetic process / seed germination / regulation of stomatal movement / plant-type vacuole / vacuole / vacuolar membrane / monoatomic ion channel complex / voltage-gated calcium channel activity / bioluminescence / generation of precursor metabolites and energy / calcium-mediated signaling / calcium ion transport / calcium ion binding / Golgi apparatus / identical protein binding / plasma membrane / cytosol 類似検索 - 分子機能
Two pore calcium channel protein 1, plant / Voltage-dependent channel domain superfamily / Green fluorescent protein, GFP / Green fluorescent protein-related / Green fluorescent protein / Green fluorescent protein / EF-hand, calcium binding motif / EF-hand calcium-binding domain profile. / EF-hand domain / Ion transport domain ...Two pore calcium channel protein 1, plant / Voltage-dependent channel domain superfamily / Green fluorescent protein, GFP / Green fluorescent protein-related / Green fluorescent protein / Green fluorescent protein / EF-hand, calcium binding motif / EF-hand calcium-binding domain profile. / EF-hand domain / Ion transport domain / Ion transport protein / EF-hand domain pair 類似検索 - ドメイン・相同性
GFP / Two pore calcium channel protein 1 類似検索 - 構成要素
生物種
Arabidopsis thaliana (シロイヌナズナ) / Human respiratory syncytial virus (ウイルス)
National Natural Science Foundation of China (NSFC)
31870724
中国
引用
ジャーナル: Proc Natl Acad Sci U S A / 年: 2021 タイトル: Voltage-gating and cytosolic Ca activation mechanisms of two-pore channel AtTPC1. 著者: Fan Ye / Lingyi Xu / Xiaoxiao Li / Weizhong Zeng / Ninghai Gan / Cheng Zhao / Wei Yang / Youxing Jiang / Jiangtao Guo / 要旨: two-pore channel AtTPC1 is a voltage-gated, Ca-modulated, nonselective cation channel that is localized in the vacuolar membrane and responsible for generating slow vacuolar (SV) current. Under ... two-pore channel AtTPC1 is a voltage-gated, Ca-modulated, nonselective cation channel that is localized in the vacuolar membrane and responsible for generating slow vacuolar (SV) current. Under depolarizing membrane potential, cytosolic Ca activates AtTPC1 by binding at the EF-hand domain, whereas luminal Ca inhibits the channel by stabilizing the voltage-sensing domain II (VSDII) in the resting state. Here, we present 2.8 to 3.3 Å cryoelectron microscopy (cryo-EM) structures of AtTPC1 in two conformations, one in closed conformation with unbound EF-hand domain and resting VSDII and the other in a partially open conformation with Ca-bound EF-hand domain and activated VSDII. Structural comparison between the two different conformations allows us to elucidate the structural mechanisms of voltage gating, cytosolic Ca activation, and their coupling in AtTPC1. This study also provides structural insight into the general voltage-gating mechanism among voltage-gated ion channels.