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Structure paper

TitleStructural basis for inositol pyrophosphate gating of the phosphate channel XPR1.
Journal, issue, pagesScience, Vol. 386, Issue 6723, Page eadp3252, Year 2024
Publish dateNov 15, 2024
AuthorsYi Lu / Chen-Xi Yue / Li Zhang / Deqiang Yao / Ying Xia / Qing Zhang / Xinchen Zhang / Shaobai Li / Yafeng Shen / Mi Cao / Chang-Run Guo / An Qin / Jie Zhao / Lu Zhou / Ye Yu / Yu Cao /
PubMed AbstractPrecise regulation of intracellular phosphate (Pi) is critical for cellular function, with xenotropic and polytropic retrovirus receptor 1 (XPR1) serving as the sole Pi exporter in humans. The ...Precise regulation of intracellular phosphate (Pi) is critical for cellular function, with xenotropic and polytropic retrovirus receptor 1 (XPR1) serving as the sole Pi exporter in humans. The mechanism of Pi efflux, activated by inositol pyrophosphates (PP-IPs), has remained unclear. This study presents cryo-electron microscopy structures of XPR1 in multiple conformations, revealing a transmembrane pathway for Pi export and a dual-binding activation pattern for PP-IPs. A canonical binding site is located at the dimeric interface of Syg1/Pho81/XPR1 (SPX) domains, and a second site, biased toward PP-IPs, is found between the transmembrane and SPX domains. By integrating structural studies with electrophysiological analyses, we characterized XPR1 as an inositol phosphates (IPs)/PP-IPs-activated phosphate channel. The interplay among its transmembrane domains, SPX domains, and IPs/PP-IPs orchestrates the conformational transition between its closed and open states.
External linksScience / PubMed:39325866
MethodsEM (single particle)
Resolution2.86 - 4.59 Å
Structure data

39203

8yet

EMDB-39203, PDB-8yet:
Cryo EM structure of human phosphate channel XPR1 in complex with IP6
Method: EM (single particle) / Resolution: 4.16 Å

39204

8yex

EMDB-39204, PDB-8yex:
Cryo EM structure of human phosphate channel XPR1 at apo state
Method: EM (single particle) / Resolution: 3.68 Å

39210

8yf4

EMDB-39210, PDB-8yf4:
Cryo EM structure of human phosphate channel XPR1 at open and inward-facing state
Method: EM (single particle) / Resolution: 3.41 Å

39220

8yfd

EMDB-39220, PDB-8yfd:
Cryo EM structure of human phosphate channel XPR1 at open state
Method: EM (single particle) / Resolution: 3.57 Å

39230

8yfu

EMDB-39230, PDB-8yfu:
Cryo EM structure of human phosphate channel XPR1 at intermediate state
Method: EM (single particle) / Resolution: 4.59 Å

39231

8yfw

EMDB-39231, PDB-8yfw:
Cryo EM structure of human phosphate channel XPR1 at intermediate state
Method: EM (single particle) / Resolution: 3.65 Å

39232

8yfx

EMDB-39232, PDB-8yfx:
Cryo EM structure of human phosphate channel XPR1 at inward-facing state
Method: EM (single particle) / Resolution: 3.56 Å

60962

9iws

EMDB-60962, PDB-9iws:
Cryo EM structure of human phosphate channel XPR1 in complex with IP7
Method: EM (single particle) / Resolution: 2.86 Å

Chemicals

ChemComp-IHP:
INOSITOL HEXAKISPHOSPHATE

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

ChemComp-I7P:
(1r,2R,3S,4s,5R,6S)-2,3,4,5,6-pentakis(phosphonooxy)cyclohexyl trihydrogen diphosphate

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / phosphate channel / INOSITOL HEXAKISPHOSPHATE / membrane protein / phosphate homeostasis / INOSITOL PYROSPHOSPHATE

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