Cryo-EM structures of human STEAP4 reveal mechanism of iron(III) reduction

Enzymes of the six-transmembrane epithelial antigen of the prostate (STEAP) family reduce Fe3+ and Cu2+ ions to facilitate metal-ion uptake by mammalian cells. Here, authors employ single-particle cryo-EM to gain insights into the molecular principles of iron reduction by human STEAP4 .

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Autores principales:	Wout Oosterheert, Laura S. van Bezouwen, Remco N. P. Rodenburg, Joke Granneman, Friedrich Förster, Andrea Mattevi, Piet Gros
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/0327e5d4fe7d44afad92e8cf690996b4
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spelling	oai:doaj.org-article:0327e5d4fe7d44afad92e8cf690996b42021-12-02T17:32:03ZCryo-EM structures of human STEAP4 reveal mechanism of iron(III) reduction10.1038/s41467-018-06817-72041-1723https://doaj.org/article/0327e5d4fe7d44afad92e8cf690996b42018-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-06817-7https://doaj.org/toc/2041-1723Enzymes of the six-transmembrane epithelial antigen of the prostate (STEAP) family reduce Fe3+ and Cu2+ ions to facilitate metal-ion uptake by mammalian cells. Here, authors employ single-particle cryo-EM to gain insights into the molecular principles of iron reduction by human STEAP4 .Wout OosterheertLaura S. van BezouwenRemco N. P. RodenburgJoke GrannemanFriedrich FörsterAndrea MatteviPiet GrosNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-9 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Wout Oosterheert Laura S. van Bezouwen Remco N. P. Rodenburg Joke Granneman Friedrich Förster Andrea Mattevi Piet Gros Cryo-EM structures of human STEAP4 reveal mechanism of iron(III) reduction
description	Enzymes of the six-transmembrane epithelial antigen of the prostate (STEAP) family reduce Fe3+ and Cu2+ ions to facilitate metal-ion uptake by mammalian cells. Here, authors employ single-particle cryo-EM to gain insights into the molecular principles of iron reduction by human STEAP4 .
format	article
author	Wout Oosterheert Laura S. van Bezouwen Remco N. P. Rodenburg Joke Granneman Friedrich Förster Andrea Mattevi Piet Gros
author_facet	Wout Oosterheert Laura S. van Bezouwen Remco N. P. Rodenburg Joke Granneman Friedrich Förster Andrea Mattevi Piet Gros
author_sort	Wout Oosterheert
title	Cryo-EM structures of human STEAP4 reveal mechanism of iron(III) reduction
title_short	Cryo-EM structures of human STEAP4 reveal mechanism of iron(III) reduction
title_full	Cryo-EM structures of human STEAP4 reveal mechanism of iron(III) reduction
title_fullStr	Cryo-EM structures of human STEAP4 reveal mechanism of iron(III) reduction
title_full_unstemmed	Cryo-EM structures of human STEAP4 reveal mechanism of iron(III) reduction
title_sort	cryo-em structures of human steap4 reveal mechanism of iron(iii) reduction
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/0327e5d4fe7d44afad92e8cf690996b4
work_keys_str_mv	AT woutoosterheert cryoemstructuresofhumansteap4revealmechanismofironiiireduction AT laurasvanbezouwen cryoemstructuresofhumansteap4revealmechanismofironiiireduction AT remconprodenburg cryoemstructuresofhumansteap4revealmechanismofironiiireduction AT jokegranneman cryoemstructuresofhumansteap4revealmechanismofironiiireduction AT friedrichforster cryoemstructuresofhumansteap4revealmechanismofironiiireduction AT andreamattevi cryoemstructuresofhumansteap4revealmechanismofironiiireduction AT pietgros cryoemstructuresofhumansteap4revealmechanismofironiiireduction
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Cryo-EM structures of human STEAP4 reveal mechanism of iron(III) reduction

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