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Structural basis of ion transport and inhibition in ferroportin.

Abstract：

:Ferroportin is an iron exporter essential for releasing cellular iron into circulation. Ferroportin is inhibited by a peptide hormone, hepcidin. In humans, mutations in ferroportin lead to ferroportin diseases that are often associated with accumulation of iron in macrophages and symptoms of iron deficiency anemia. Here we present the structures of the ferroportin from the primate Philippine tarsier (TsFpn) in the presence and absence of hepcidin solved by cryo-electron microscopy. TsFpn is composed of two domains resembling a clamshell and the structure defines two metal ion binding sites, one in each domain. Both structures are in an outward-facing conformation, and hepcidin binds between the two domains and reaches one of the ion binding sites. Functional studies show that TsFpn is an electroneutral H+/Fe2+ antiporter so that transport of each Fe2+ is coupled to transport of two H+ in the opposite direction. Perturbing either of the ion binding sites compromises the coupled transport of H+ and Fe2+. These results establish the structural basis of metal ion binding, transport and inhibition in ferroportin and provide a blueprint for targeting ferroportin in pharmacological intervention of ferroportin diseases.

journal_name

Nat Commun

journal_title

Nature communications

authors

Pan Y,Ren Z,Gao S,Shen J,Wang L,Xu Z,Yu Y,Bachina P,Zhang H,Fan X,Laganowsky A,Yan N,Zhou M

doi

10.1038/s41467-020-19458-6

subject

Has Abstract

pub_date

2020-11-10 00:00:00

pages

5686

issue

1

issn

2041-1723

pii

10.1038/s41467-020-19458-6

journal_volume

11

pub_type

杂志文章

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