EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Structural insights into human zinc transporter ZnT1 mediated Zn efflux.
ジャーナル・号・ページ	EMBO Rep, Vol. 25, Issue 11, Page 5006-5025, Year 2024
掲載日	2024年10月10日
著者	Yonghui Long / Zhini Zhu / Zixuan Zhou / Chuanhui Yang / Yulin Chao / Yuwei Wang / Qingtong Zhou / Ming-Wei Wang / Qianhui Qu /
PubMed 要旨	Zinc transporter 1 (ZnT1), the principal carrier of cytosolic zinc to the extracellular milieu, is important for cellular zinc homeostasis and resistance to zinc toxicity. Despite recent advancements ...Zinc transporter 1 (ZnT1), the principal carrier of cytosolic zinc to the extracellular milieu, is important for cellular zinc homeostasis and resistance to zinc toxicity. Despite recent advancements in the structural characterization of various zinc transporters, the mechanism by which ZnTs-mediated Zn translocation is coupled with H or Ca remains unclear. To visualize the transport dynamics, we determined the cryo-electron microscopy (cryo-EM) structures of human ZnT1 at different functional states. ZnT1 dimerizes via extensive interactions between the cytosolic (CTD), the transmembrane (TMD), and the unique cysteine-rich extracellular (ECD) domains. At pH 7.5, both protomers adopt an outward-facing (OF) conformation, with Zn ions coordinated at the TMD binding site by distinct compositions. At pH 6.0, ZnT1 complexed with Zn exhibits various conformations [OF/OF, OF/IF (inward-facing), and IF/IF]. These conformational snapshots, together with biochemical investigation and molecular dynamic simulations, shed light on the mechanism underlying the proton-dependence of ZnT1 transport.
リンク	EMBO Rep / PubMed:39390258 / PubMed Central
手法	EM (単粒子)
解像度	2.65 - 4.18 Å
構造データ	38465 8xm6 EMDB-38465, PDB-8xm6: Cryo-EM structure of human ZnT1 WT, in the absence of zinc, determined in an outward-facing conformation 手法: EM (単粒子) / 解像度: 3.48 Å 38469 8xma EMDB-38469, PDB-8xma: Cryo-EM structure of human ZnT1 WT, in the presence of zinc, determined in an outward-facing conformation 手法: EM (単粒子) / 解像度: 2.65 Å EMDB-38474: Cryo-EM structure of human ZnT1 WT at a low PH, in the presence of zinc, determined in an outward-facing conformation. 手法: EM (単粒子) / 解像度: 3.7 Å 38475 8xmf EMDB-38475, PDB-8xmf: Cryo-EM structure of human ZnT1 WT at a low PH, in the presence of zinc, determined in an inward-facing conformation. 手法: EM (単粒子) / 解像度: 3.64 Å 38479 8xmj EMDB-38479, PDB-8xmj: Cryo-EM structure of human ZnT1 WT, in the presence of zinc, determined in heterogeneous conformations- one subunit in an inward-facing and the other in an outward-facing conformation 手法: EM (単粒子) / 解像度: 4.18 Å 38494 8xn1 EMDB-38494, PDB-8xn1: Cryo-EM structure of human ZnT3, in the presence of zinc, determined in an inward-facing conformation 手法: EM (単粒子) / 解像度: 3.14 Å
化合物	ChemComp-ZN: Unknown entry ChemComp-AV0: Lauryl Maltose Neopentyl Glycol / ラウリルマルト-スネオペンチルグリコ-ル ChemComp-Y01: CHOLESTEROL HEMISUCCINATE / コレステリルヘミスクシナ-ト PDB-1l42: CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY
由来	homo sapiens (ヒト)
キーワード	TRANSPORT PROTEIN / Human ZnT1 / Zinc transpoter / Outward-facing conformation / Inward-facing conformation / transpost protein / Heterogenous dimeric conformation / Human ZnT3 / inward- facing conformation / transport ptotein.