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TitleHuman XPR1 structures reveal phosphate export mechanism.
Journal, issue, pagesNature, Vol. 633, Issue 8031, Page 960-967, Year 2024
Publish dateAug 21, 2024
AuthorsRui Yan / Huiwen Chen / Chuanyu Liu / Jun Zhao / Di Wu / Juquan Jiang / Jianke Gong / Daohua Jiang /
PubMed AbstractInorganic phosphate (Pi) is a fundamental macronutrient for all living organisms, the homeostasis of which is critical for numerous biological activities. As the only known human Pi exporter to date, ...Inorganic phosphate (Pi) is a fundamental macronutrient for all living organisms, the homeostasis of which is critical for numerous biological activities. As the only known human Pi exporter to date, XPR1 has an indispensable role in cellular Pi homeostasis. Dysfunction of XPR1 is associated with neurodegenerative disease. However, the mechanisms underpinning XPR1-mediated Pi efflux and regulation by the intracellular inositol polyphosphate (InsPP) sensor SPX domain remain poorly understood. Here we present cryo-electron microscopy structures of human XPR1 in Pi-bound closed, open and InsP-bound forms, revealing the structural basis for XPR1 gating and regulation by InsPPs. XPR1 consists of an N-terminal SPX domain, a dimer-formation core domain and a Pi transport domain. Within the transport domain, three basic clusters are responsible for Pi binding and transport, and a conserved W573 acts as a molecular switch for gating. In addition, the SPX domain binds to InsP and facilitates Pi efflux by liberating the C-terminal loop that limits Pi entry. This study provides a conceptual framework for the mechanistic understanding of Pi homeostasis by XPR1 homologues in fungi, plants and animals.
External linksNature / PubMed:39169184
MethodsEM (single particle)
Resolution2.84 - 3.61 Å
Structure data

38065

8x5b

EMDB-38065, PDB-8x5b:
Cryo-EM structures of human XPR1 in closed states
Method: EM (single particle) / Resolution: 2.84 Å

38067

8x5e

EMDB-38067, PDB-8x5e:
Cryo-EM structure of human XPR1 in open state
Method: EM (single particle) / Resolution: 3.61 Å

38068

8x5f

EMDB-38068, PDB-8x5f:
human XPR1 in complex with InsP6
Method: EM (single particle) / Resolution: 2.96 Å

Chemicals

ChemComp-PO4:
PHOSPHATE ION

ChemComp-POV:
(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate / phospholipid*YM

ChemComp-CLR:
CHOLESTEROL

ChemComp-HOH:
WATER

ChemComp-6OU:
[(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl] (~{Z})-octadec-9-enoate / phospholipid*YM

ChemComp-IHP:
INOSITOL HEXAKISPHOSPHATE

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / transport / transport open state

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