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 basis of polyamine transport by human ATP13A2 (PARK9).
Journal, issue, pages	Mol Cell, Vol. 81, Issue 22, Page 4635-44649.e8, Year 2021
Publish date	Nov 18, 2021
Authors	Sue Im Sim / Sören von Bülow / Gerhard Hummer / Eunyong Park /
PubMed Abstract	Polyamines are small, organic polycations that are ubiquitous and essential to all forms of life. Currently, how polyamines are transported across membranes is not understood. Recent studies have ...Polyamines are small, organic polycations that are ubiquitous and essential to all forms of life. Currently, how polyamines are transported across membranes is not understood. Recent studies have suggested that ATP13A2 and its close homologs, collectively known as P5B-ATPases, are polyamine transporters at endo-/lysosomes. Loss-of-function mutations of ATP13A2 in humans cause hereditary early-onset Parkinson's disease. To understand the polyamine transport mechanism of ATP13A2, we determined high-resolution cryoelectron microscopy (cryo-EM) structures of human ATP13A2 in five distinct conformational intermediates, which together, represent a near-complete transport cycle of ATP13A2. The structural basis of the polyamine specificity was revealed by an endogenous polyamine molecule bound to a narrow, elongated cavity within the transmembrane domain. The structures show an atypical transport path for a water-soluble substrate, in which polyamines may exit within the cytosolic leaflet of the membrane. Our study provides important mechanistic insights into polyamine transport and a framework to understand the functions and mechanisms of P5B-ATPases.
External links	Mol Cell / PubMed:34715013 / PubMed Central
Methods	EM (single particle)
Resolution	2.5 - 3.7 Å
Structure data	EMDB-24212: Cryo-EM structure of ATP13A2 in the E2-Pi state Method: EM (single particle) / Resolution: 3.7 Å EMDB-24213: Cryo-EM structure of ATP13A2 in the E2-Pi state Method: EM (single particle) / Resolution: 3.2 Å 24214 7n70 EMDB-24214, PDB-7n70: Cryo-EM structure of ATP13A2 in the BeF-bound E2P-like state Method: EM (single particle) / Resolution: 2.8 Å EMDB-24215: Cryo-EM structure of ATP13A2 in the E2-Pi state Method: EM (single particle) / Resolution: 3.1 Å EMDB-24216: Cryo-EM structure of ATP13A2 in the AlF-bound E2-Pi-like state Method: EM (single particle) / Resolution: 2.8 Å 24217 7n72 EMDB-24217, PDB-7n72: Cryo-EM structure of ATP13A2 in the AlF-bound E2-Pi-like state Method: EM (single particle) / Resolution: 2.5 Å 24218 7n73 EMDB-24218, PDB-7n73: Cryo-EM structure of ATP13A2 in the ADP-AlF-bound E1P-ADP-like state Method: EM (single particle) / Resolution: 2.9 Å 24219 7n74 EMDB-24219, PDB-7n74: Cryo-EM structure of ATP13A2 D508N mutant in the E1-ATP-like state Method: EM (single particle) / Resolution: 2.8 Å 24220 7n75 EMDB-24220, PDB-7n75: Cryo-EM structure of ATP13A2 D458N/D962N mutant in the E1-apo state, Conformation 1 Method: EM (single particle) / Resolution: 2.9 Å 24221 7n76 EMDB-24221, PDB-7n76: Cryo-EM structure of ATP13A2 D458N/D962N mutant in the E1-apo state, Conformation 2 Method: EM (single particle) / Resolution: 2.9 Å 24222 7n77 EMDB-24222, PDB-7n77: Cryo-EM structure of ATP13A2 D458N/D962N mutant in the AlF-bound E1P-like state Method: EM (single particle) / Resolution: 3.2 Å 24223 7n78 EMDB-24223, PDB-7n78: Cryo-EM structure of ATP13A2 in the E2-Pi state Method: EM (single particle) / Resolution: 3.0 Å
Chemicals	ChemComp-BEF: BERYLLIUM TRIFLUORIDE ION ChemComp-MG: Unknown entry ChemComp-Y01: CHOLESTEROL HEMISUCCINATE ChemComp-LMT: DODECYL-BETA-D-MALTOSIDE / detergentYM ChemComp-ALF: TETRAFLUOROALUMINATE ION ChemComp-SPM: SPERMINE ChemComp-PC1: 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipidYM ChemComp-HOH: WATER ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-PO4: PHOSPHATE ION
Source	homo sapiens (human)
Keywords	TRANSPORT PROTEIN / P-type ATPase / P5B-ATPase / polyamine transporter