- EMDB-36055: Cryo-EM structure of hZnT7-Fab complex in zinc state 1, determine... -
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データベース: EMDB / ID: EMD-36055
タイトル
Cryo-EM structure of hZnT7-Fab complex in zinc state 1, determined in heterogeneous conformations- one subunit in an inward-facing zinc-bound and the other in an outward-facing zinc-unbound conformation
マップデータ
試料
複合体: Human ZnT7-Fab complex
タンパク質・ペプチド: Zinc transporter 7
タンパク質・ペプチド: Light chain of YN7114-08 Fab
タンパク質・ペプチド: Heavy chain of YN7114-08 Fab
リガンド: ZINC ION
キーワード
zinc / proton / transporter / Golgi apparatus / metal transporter / histidine-rich loop / METAL TRANSPORT
機能・相同性
機能・相同性情報
zinc ion import into Golgi lumen / Golgi cis cisterna membrane / zinc ion transmembrane transporter activity / intracellular zinc ion homeostasis / sarcoplasmic reticulum membrane / cytoplasmic vesicle / vesicle / Golgi membrane / perinuclear region of cytoplasm / Golgi apparatus ...zinc ion import into Golgi lumen / Golgi cis cisterna membrane / zinc ion transmembrane transporter activity / intracellular zinc ion homeostasis / sarcoplasmic reticulum membrane / cytoplasmic vesicle / vesicle / Golgi membrane / perinuclear region of cytoplasm / Golgi apparatus / mitochondrion / identical protein binding / cytoplasm 類似検索 - 分子機能
Zinc transporter Msc2-like / Cation efflux protein / Cation efflux transmembrane domain superfamily / Cation efflux family 類似検索 - ドメイン・相同性
Ministry of Education, Culture, Sports, Science and Technology (Japan)
18H03978
日本
Ministry of Education, Culture, Sports, Science and Technology (Japan)
21H04758
日本
Ministry of Education, Culture, Sports, Science and Technology (Japan)
21H05247
日本
引用
ジャーナル: Nat Commun / 年: 2023 タイトル: Cryo-EM structures of human zinc transporter ZnT7 reveal the mechanism of Zn uptake into the Golgi apparatus. 著者: Han Ba Bui / Satoshi Watanabe / Norimichi Nomura / Kehong Liu / Tomoko Uemura / Michio Inoue / Akihisa Tsutsumi / Hiroyuki Fujita / Kengo Kinoshita / Yukinari Kato / So Iwata / Masahide Kikkawa / Kenji Inaba / 要旨: Zinc ions (Zn) are vital to most cells, with the intracellular concentrations of Zn being tightly regulated by multiple zinc transporters located at the plasma and organelle membranes. We herein ...Zinc ions (Zn) are vital to most cells, with the intracellular concentrations of Zn being tightly regulated by multiple zinc transporters located at the plasma and organelle membranes. We herein present the 2.2-3.1 Å-resolution cryo-EM structures of a Golgi-localized human Zn/H antiporter ZnT7 (hZnT7) in Zn-bound and unbound forms. Cryo-EM analyses show that hZnT7 exists as a dimer via tight interactions in both the cytosolic and transmembrane (TM) domains of two protomers, each of which contains a single Zn-binding site in its TM domain. hZnT7 undergoes a TM-helix rearrangement to create a negatively charged cytosolic cavity for Zn entry in the inward-facing conformation and widens the luminal cavity for Zn release in the outward-facing conformation. An exceptionally long cytosolic histidine-rich loop characteristic of hZnT7 binds two Zn ions, seemingly facilitating Zn recruitment to the TM metal transport pathway. These structures permit mechanisms of hZnT7-mediated Zn uptake into the Golgi to be proposed.