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	Conformational cycle of human polyamine transporter ATP13A2.
Journal, issue, pages	Nat Commun, Vol. 14, Issue 1, Page 1978, Year 2023
Publish date	Apr 8, 2023
Authors	Jianqiang Mu / Chenyang Xue / Lei Fu / Zongjun Yu / Minhan Nie / Mengqi Wu / Xinmeng Chen / Kun Liu / Ruiqian Bu / Ying Huang / Baisheng Yang / Jianming Han / Qianru Jiang / Kevin C Chan / Ruhong Zhou / Huilin Li / Ancheng Huang / Yong Wang / Zhongmin Liu /
PubMed Abstract	Dysregulation of polyamine homeostasis strongly associates with human diseases. ATP13A2, which is mutated in juvenile-onset Parkinson's disease and autosomal recessive spastic paraplegia 78, is a ...Dysregulation of polyamine homeostasis strongly associates with human diseases. ATP13A2, which is mutated in juvenile-onset Parkinson's disease and autosomal recessive spastic paraplegia 78, is a transporter with a critical role in balancing the polyamine concentration between the lysosome and the cytosol. Here, to better understand human ATP13A2-mediated polyamine transport, we use single-particle cryo-electron microscopy to solve high-resolution structures of human ATP13A2 in six intermediate states, including the putative E2 structure for the P5 subfamily of the P-type ATPases. These structures comprise a nearly complete conformational cycle spanning the polyamine transport process and capture multiple substrate binding sites distributed along the transmembrane regions, suggesting a potential polyamine transport pathway. Integration of high-resolution structures, biochemical assays, and molecular dynamics simulations allows us to obtain a better understanding of the structural basis of how hATP13A2 transports polyamines, providing a mechanistic framework for ATP13A2-related diseases.
External links	Nat Commun / PubMed:37031211 / PubMed Central
Methods	EM (single particle)
Resolution	3.2 - 5.65 Å
Structure data	35384 8iek EMDB-35384, PDB-8iek: Cryo-EM structure of ATP13A2 in the E1-ATP state Method: EM (single particle) / Resolution: 3.2 Å 35385 8iel EMDB-35385, PDB-8iel: Cryo-EM structure of ATP13A2 in the E1-like state Method: EM (single particle) / Resolution: 5.65 Å 35386 8iem EMDB-35386, PDB-8iem: Cryo-EM structure of ATP13A2 in the E2P state Method: EM (single particle) / Resolution: 3.35 Å 35387 8ien EMDB-35387, PDB-8ien: Cryo-EM structure of ATP13A2 in the E2-Pi state Method: EM (single particle) / Resolution: 3.25 Å 35388 8ieo EMDB-35388, PDB-8ieo: Cryo-EM structure of ATP13A2 in the nominal E1P state Method: EM (single particle) / Resolution: 3.78 Å 35391 8ier EMDB-35391, PDB-8ier: Cryo-EM structure of ATP13A2 in the putative of E2 state Method: EM (single particle) / Resolution: 4.87 Å 35392 8ies EMDB-35392, PDB-8ies: Cryo-EM structure of ATP13A2 in the E1P-ADP state Method: EM (single particle) / Resolution: 3.73 Å
Chemicals	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-MG: Unknown entry ChemComp-SPM: SPERMINE ChemComp-BEF: BERYLLIUM TRIFLUORIDE ION ChemComp-ALF: TETRAFLUOROALUMINATE ION ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM
Source	homo sapiens (human)
Keywords	PROTEIN TRANSPORT / Cryo-EM structure of ATP13A2 in the E1-ATP state; Membran protein / Cryo-EM structure of ATP13A2 in the E1-like state / membrane protein / Cryo-EM structure of ATP13A2 in the E2P state; Membran protein / TRANSPORT PROTEIN / Cryo-EM structure of ATP13A2 in the E2-Pi state / Cryo-EM structure of ATP13A2 in the nominal E1P state; Membrane protein / Cryo-EM structure of ATP13A2 in the putative of E2 state; Membrane protein / Cryo-EM structure of ATP13A2 in the E1P-ADP state; Membrane protein