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Structure paper

TitleStructure of hepcidin-bound ferroportin reveals iron homeostatic mechanisms.
Journal, issue, pagesNature, Vol. 586, Issue 7831, Page 807-811, Year 2020
Publish dateAug 19, 2020
AuthorsChristian B Billesbølle / Caleigh M Azumaya / Rachael C Kretsch / Alexander S Powers / Shane Gonen / Simon Schneider / Tara Arvedson / Ron O Dror / Yifan Cheng / Aashish Manglik /
PubMed AbstractThe serum level of iron in humans is tightly controlled by the action of the hormone hepcidin on the iron efflux transporter ferroportin. Hepcidin regulates iron absorption and recycling by inducing ...The serum level of iron in humans is tightly controlled by the action of the hormone hepcidin on the iron efflux transporter ferroportin. Hepcidin regulates iron absorption and recycling by inducing the internalization and degradation of ferroportin. Aberrant ferroportin activity can lead to diseases of iron overload, such as haemochromatosis, or iron limitation anaemias. Here we determine cryogenic electron microscopy structures of ferroportin in lipid nanodiscs, both in the apo state and in complex with hepcidin and the iron mimetic cobalt. These structures and accompanying molecular dynamics simulations identify two metal-binding sites within the N and C domains of ferroportin. Hepcidin binds ferroportin in an outward-open conformation and completely occludes the iron efflux pathway to inhibit transport. The carboxy terminus of hepcidin directly contacts the divalent metal in the ferroportin C domain. Hepcidin binding to ferroportin is coupled to iron binding, with an 80-fold increase in hepcidin affinity in the presence of iron. These results suggest a model for hepcidin regulation of ferroportin, in which only ferroportin molecules loaded with iron are targeted for degradation. More broadly, our structural and functional insights may enable more targeted manipulation of the hepcidin-ferroportin axis in disorders of iron homeostasis.
External linksNature / PubMed:32814342 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.1 - 3.2 Å
Structure data

21539

6w4s

EMDB-21539, PDB-6w4s:
Structure of apo human ferroportin in lipid nanodisc
Method: EM (single particle) / Resolution: 3.2 Å

21599

6wbv

EMDB-21599, PDB-6wbv:
Structure of human ferroportin bound to hepcidin and cobalt in lipid nanodisc
Method: EM (single particle) / Resolution: 2.5 Å

PDB-6w4v:
Structure of anti-ferroportin Fab45D8
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL / Ethylene glycol

ChemComp-HOH:
WATER / Water

ChemComp-AGA:
(1S)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PENTANOYLOXY)METHYL]ETHYL OCTANOATE

ChemComp-CO:
Unknown entry

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsTRANSPORT PROTEIN/IMMUNE SYSTEM / ferroportin / transporter / iron / hepcidin / TRANSPORT PROTEIN-IMMUNE SYSTEM complex / IMMUNE SYSTEM / antibody / Fab / TRANSLOCASE/IMMUNE SYSTEM/HORMONE / TRANSLOCASE-IMMUNE SYSTEM-HORMONE complex

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