+
Open data
-
Basic information
Entry | ![]() | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Complex of XPR1-KIDINS220 | |||||||||
![]() | ||||||||||
![]() |
| |||||||||
![]() | phosphate channel / TRANSPORT PROTEIN | |||||||||
Function / homology | ![]() phosphate transmembrane transporter activity / nerve growth factor signaling pathway / phosphate ion transport / intracellular phosphate ion homeostasis / ARMS-mediated activation / phosphate ion transmembrane transport / cellular response to phosphate starvation / protein kinase regulator activity / inositol hexakisphosphate binding / RND1 GTPase cycle ...phosphate transmembrane transporter activity / nerve growth factor signaling pathway / phosphate ion transport / intracellular phosphate ion homeostasis / ARMS-mediated activation / phosphate ion transmembrane transport / cellular response to phosphate starvation / protein kinase regulator activity / inositol hexakisphosphate binding / RND1 GTPase cycle / RND2 GTPase cycle / dendrite morphogenesis / efflux transmembrane transporter activity / PDZ domain binding / positive regulation of neuron projection development / cellular response to nerve growth factor stimulus / response to virus / late endosome / virus receptor activity / in utero embryonic development / protein-containing complex / membrane / plasma membrane / cytosol Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.44 Å | |||||||||
![]() | Wang X / Bai Z / Wallis C / Wang H / Han Y / Jin R / Lei M / Gu C / Jessen H / Shears S ...Wang X / Bai Z / Wallis C / Wang H / Han Y / Jin R / Lei M / Gu C / Jessen H / Shears S / Sun Y / Corry B / Zhang Y | |||||||||
Funding support | ![]()
| |||||||||
![]() | ![]() Title: KIDINS220 and InsP8 safeguard the stepwise regulation of phosphate exporter XPR1. 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 / ![]() ![]() ![]() ![]() 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. | |||||||||
History |
|
-
Structure visualization
Supplemental images |
---|
-
Downloads & links
-EMDB archive
Map data | ![]() | 265.3 MB | ![]() | |
---|---|---|---|---|
Header (meta data) | ![]() ![]() | 15.5 KB 15.5 KB | Display Display | ![]() |
Images | ![]() | 116 KB | ||
Filedesc metadata | ![]() | 6.4 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 391 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 390.6 KB | Display | |
Data in XML | ![]() | 4.3 KB | Display | |
Data in CIF | ![]() | 5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9jxqMC ![]() 9jxdC ![]() 9jxeC ![]() 9jxfC ![]() 9jxgC ![]() 9jxhC ![]() 9jxiC ![]() 9jxjC ![]() 9jxkC ![]() 9jxlC ![]() 9jxmC ![]() 9jxnC ![]() 9jxoC ![]() 9jxpC ![]() 9jxrC C: citing same article ( M: atomic model generated by this map |
---|---|
Similar structure data | Similarity search - Function & homology ![]() |
-
Links
EMDB pages | ![]() ![]() |
---|---|
Related items in Molecule of the Month |
-
Map
File | ![]() | ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & slices | Image control
Images are generated by Spider. generated in cubic-lattice coordinate | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.055 Å | ||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
|
-Supplemental data
-
Sample components
-Entire : Complex of XPR1-KIDINS220
Entire | Name: Complex of XPR1-KIDINS220 |
---|---|
Components |
|
-Supramolecule #1: Complex of XPR1-KIDINS220
Supramolecule | Name: Complex of XPR1-KIDINS220 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #2, #1 |
---|---|
Source (natural) | Organism: ![]() |
-Macromolecule #1: Solute carrier family 53 member 1
Macromolecule | Name: Solute carrier family 53 member 1 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 76.823562 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MKFAEHLSAH ITPEWRKQYI QYEAFKDMLY SAQDQAPSVE VTDEDTVKRY FAKFEEKFFQ TCEKELAKIN TFYSEKLAEA QRRFATLQN ELQSSLDAQK ESTGVTTLRQ RRKPVFHLSH EERVQHRNIK DLKLAFSEFY LSLILLQNYQ NLNFTGFRKI L KKHDKILE ...String: MKFAEHLSAH ITPEWRKQYI QYEAFKDMLY SAQDQAPSVE VTDEDTVKRY FAKFEEKFFQ TCEKELAKIN TFYSEKLAEA QRRFATLQN ELQSSLDAQK ESTGVTTLRQ RRKPVFHLSH EERVQHRNIK DLKLAFSEFY LSLILLQNYQ NLNFTGFRKI L KKHDKILE TSRGADWRVA HVEVAPFYTC KKINQLISET EAVVTNELED GDRQKAMKRL RVPPLGAAQP APAWTTFRVG LF CGIFIVL NITLVLAAVF KLETDRSIWP LIRIYRGGFL LIEFLFLLGI NTYGWRQAGV NHVLIFELNP RSNLSHQHLF EIA GFLGIL WCLSLLACFF APISVIPTYV YPLALYGFMV FFLINPTKTF YYKSRFWLLK LLFRVFTAPF HKVGFADFWL ADQL NSLSV ILMDLEYMIC FYSLELKWDE SKGLLPNNSE ESGICHKYTY GVRAIVQCIP AWLRFIQCLR RYRDTKRAFP HLVNA GKYS TTFFMVTFAA LYSTHKERGH SDTMVFFYLW IVFYIISSCY TLIWDLKMDW GLFDKNAGEN TFLREEIVYP QKAYYY CAI IEDVILRFAW TIQISITSTT LLPHSGDIIA TVFAPLEVFR RFVWNFFRLE NEHLNNCGEF RAVRDISVAP LNADDQT LL EQMMDQDDGV RNR UniProtKB: Solute carrier family 53 member 1 |
-Macromolecule #2: Kinase D-interacting substrate of 220 kDa
Macromolecule | Name: Kinase D-interacting substrate of 220 kDa / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 43.367641 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: VDERNECGQT PLMIAAEQGN LEIVKELIKN GANCNLEDLD NWTALISASK EGHVHIVEEL LKCGVNLEHR DMGGWTALMW ACYKGRTDV VELLLSHGAN PSVTGLYSVY PIIWAAGRGH ADIVHLLLQN GAKVNCSDKY GTTPLVWAAR KGHLECVKHL L AMGADVDQ ...String: VDERNECGQT PLMIAAEQGN LEIVKELIKN GANCNLEDLD NWTALISASK EGHVHIVEEL LKCGVNLEHR DMGGWTALMW ACYKGRTDV VELLLSHGAN PSVTGLYSVY PIIWAAGRGH ADIVHLLLQN GAKVNCSDKY GTTPLVWAAR KGHLECVKHL L AMGADVDQ EGANSMTALI VAVKGGYTQS VKEILKRNPN VNLTDKDGNT ALMIASKEGH TEIVQDLLDA GTYVNIPDRS GD TVLIGAV RGGHVEIVRA LLQKYADIDI RGQDNKTALY WAVEKGNATM VRDILQCNPD TEICTKDGET PLIKATKMRN IEV VELLLD KGAKVSAVDK KGDTPLHIAI RGRSRKLAEL LLRNPKDGRL LYRPNKAGET PYNIDCSHQK SILTQIFGAR UniProtKB: Kinase D-interacting substrate of 220 kDa |
-Experimental details
-Structure determination
Method | cryo EM |
---|---|
![]() | single particle reconstruction |
Aggregation state | particle |
-
Sample preparation
Buffer | pH: 7.4 |
---|---|
Vitrification | Cryogen name: ETHANE |
-
Electron microscopy
Microscope | TFS KRIOS |
---|---|
Image recording | Film or detector model: GATAN K3 BIOCONTINUUM (6k x 4k) / Average electron dose: 49.41 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 1.4000000000000001 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |