Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structural insights into human zinc transporter ZnT1 mediated Zn efflux.
Journal, issue, pages	EMBO Rep, Year 2024
Publish date	Oct 10, 2024
Authors	Yonghui Long / Zhini Zhu / Zixuan Zhou / Chuanhui Yang / Yulin Chao / Yuwei Wang / Qingtong Zhou / Ming-Wei Wang / Qianhui Qu /
PubMed Abstract	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.
External links	EMBO Rep / PubMed:39390258
Methods	EM (single particle)
Resolution	2.65 - 4.18 Å
Structure data	38465 8xm6 EMDB-38465, PDB-8xm6: Cryo-EM structure of human ZnT1 WT, in the absence of zinc, determined in an outward-facing conformation Method: EM (single particle) / Resolution: 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 Method: EM (single particle) / Resolution: 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. Method: EM (single particle) / Resolution: 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. Method: EM (single particle) / Resolution: 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 Method: EM (single particle) / Resolution: 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 Method: EM (single particle) / Resolution: 3.14 Å
Chemicals	ChemComp-ZN: Unknown entry ChemComp-AV0: Lauryl Maltose Neopentyl Glycol ChemComp-Y01: CHOLESTEROL HEMISUCCINATE PDB-1l42: CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY
Source	homo sapiens (human)
Keywords	TRANSPORT PROTEIN / Human ZnT1 / Zinc transpoter / Outward-facing conformation / Inward-facing conformation / transpost protein / Heterogenous dimeric conformation / Human ZnT3 / inward- facing conformation / transport ptotein.