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	KIDINS220 and InsP8 safeguard the stepwise regulation of phosphate exporter XPR1.
Journal, issue, pages	Mol Cell, Vol. 85, Issue 17, Page 3209-33224.e8, Year 2025
Publish date	Sep 4, 2025
Authors	Xiaojie Wang / Zhongjian Bai / Ciara Wallis / Huanchen Wang / Yaoyao Han / Ruitao Jin / Mingguang Lei / Tian Yang / Chunfang Gu / Henning Jessen / Stephen Shears / Yadong Sun / Ben Corry / Yixiao Zhang /
PubMed Abstract	XPR1 is emerging as the only known inorganic phosphate (Pi) exporter in humans, critical for Pi homeostasis, with its activity stimulated by inositol pyrophosphate InsP8 and regulated by neuronal ...XPR1 is emerging as the only known inorganic phosphate (Pi) exporter in humans, critical for Pi homeostasis, with its activity stimulated by inositol pyrophosphate InsP8 and regulated by neuronal scaffold protein KIDINS220. Our structural studies reveal that InsP8 specifically activates XPR1 in a stepwise manner, involving profound SYG1/PHO/XPR1 (SPX) domain movements. Each XPR1 subunit functions with four gating states, in which Pi permeates a constriction site via a "knock-kiss-kick" process. By contrast, KIDINS220 delicately stabilizes XPR1 in a closed conformation through multiple mechanisms, one of which involves trapping the XPR1 α1 helix-critical for InsP8 binding-within an interaction hub. InsP8 serves as a key to release KIDINS220's restraint, reinforcing a "key-to-locks" mechanism to safeguard the stepwise activation. Additionally, our study provides direct structural insights into XPR1-associated neuronal disorders and highlights the evolutionary conservation and divergence among XPR1 orthologs, offering a comprehensive understanding of Pi homeostasis across species.
External links	Mol Cell / PubMed:40858110 / PubMed Central
Methods	EM (single particle)
Resolution	3.12 - 7.52 Å
Structure data	61859 9jxd EMDB-61859, PDB-9jxd: Cryo-EM structure of human XPR1 in apo state Method: EM (single particle) / Resolution: 3.29 Å 61860 9jxe EMDB-61860, PDB-9jxe: Cryo-EM structure of apo human XPR1, class 1, with one visible SPX domain Method: EM (single particle) / Resolution: 3.85 Å 61861 9jxf EMDB-61861, PDB-9jxf: Cryo-EM structure of apo human XPR1, class 2, with asymmetrically dimerized SPX domains Method: EM (single particle) / Resolution: 4.31 Å 61862 9jxg EMDB-61862, PDB-9jxg: Cryo-EM structure of apo human XPR1, class 3, with symmetrically dimerized SPX domains Method: EM (single particle) / Resolution: 3.75 Å 61863 9jxh EMDB-61863, PDB-9jxh: Cryo-EM structure of human XPR1 in complex with InsP8 Method: EM (single particle) / Resolution: 3.15 Å 61864 9jxi EMDB-61864, PDB-9jxi: Cryo-EM structure of human XPR1 with InsP8 in an 'arch-like' intermediate state of the SPX domain Method: EM (single particle) / Resolution: 3.31 Å 61865 9jxj EMDB-61865, PDB-9jxj: Cryo-EM structure of human XPR1 in a closed state at both the extracellular and intracellular gates, obtained through local refinement Method: EM (single particle) / Resolution: 3.22 Å 61866 9jxk EMDB-61866, PDB-9jxk: Cryo-EM structure of human XPR1 in a closed state at the intracellular gate and an open state at the extracellular gate, obtained through local refinement Method: EM (single particle) / Resolution: 3.38 Å 61867 9jxl EMDB-61867, PDB-9jxl: Cryo-EM structure of human XPR1 in an open state at the intracellular gate and a closed state at the extracellular gate, obtained through local refinement Method: EM (single particle) / Resolution: 3.23 Å 61868 9jxm EMDB-61868, PDB-9jxm: Cryo-EM structure of one subunit of the human XPR1 homodimer with both the intracellular and extracellular gates in an open state, obtained through local refinement Method: EM (single particle) / Resolution: 3.48 Å 61869 9jxn EMDB-61869, PDB-9jxn: Cryo-EM structure of human XPR1-R459C Method: EM (single particle) / Resolution: 3.12 Å 61870 9jxo EMDB-61870, PDB-9jxo: Cryo-EM structure of human XPR1-G621A Method: EM (single particle) / Resolution: 3.48 Å 61871 9jxp EMDB-61871, PDB-9jxp: Cryo-EM structure of human XPR1-R570L Method: EM (single particle) / Resolution: 3.53 Å EMDB-61872: Cryo-EM structure of XPR1-KIDINS220 complex Method: EM (single particle) / Resolution: 3.44 Å EMDB-61873: Local refinement of SPX and ARs in XPR1-KIDINS220 complex Method: EM (single particle) / Resolution: 3.54 Å EMDB-61874: Local refinement of additional KIDINS220 TM-helix in XPR1-KIDINS220 complex Method: EM (single particle) / Resolution: 3.75 Å 61875 9jxq EMDB-61875, PDB-9jxq: Complex of XPR1-KIDINS220 Method: EM (single particle) / Resolution: 3.44 Å EMDB-61876: Cryo-EM structure of XPR1-KIDINS220-InsP8 complex Method: EM (single particle) / Resolution: 4.47 Å 61877 9jxr EMDB-61877, PDB-9jxr: Cryo-EM structure of Drosophila melanogaster PXo-G604A Method: EM (single particle) / Resolution: 3.53 Å EMDB-61878: Cryo-EM structure of Drosophila melanogaster PXo Method: EM (single particle) / Resolution: 5.85 Å EMDB-61879: Cryo-EM structure of PHO1 Method: EM (single particle) / Resolution: 7.52 Å
Chemicals	ChemComp-I8P: (1R,3S,4R,5S,6R)-2,4,5,6-tetrakis(phosphonooxy)cyclohexane-1,3-diyl bis[trihydrogen (diphosphate)] ChemComp-HOH: WATER ChemComp-PO4: PHOSPHATE ION
Source	homo sapiens (human) drosophila melanogaster (fruit fly)
Keywords	TRANSPORT PROTEIN / phosphate channel;phosphate exporter;PFBC / phosphate channel