The crystal structure of Acinetobacter baumannii bacterioferritin reveals a heteropolymer of bacterioferritin and ferritin subunits

Autores
Yao, Huili; Alli, Suliat; Liu, Lijun; Soldano, Anabel; Cooper, Anne; Fontenot, Leo; Verdin, Dristen; Battaile, Kevin P.; Lovell, Scott; Rivera, Mario
Año de publicación
2024
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Iron storage proteins, e.g., vertebrate ferritin, and the ferritin-like bacterioferritin (Bfr) and bacterial ferritin (Ftn), are spherical, hollow proteins that catalyze the oxidation of Fe2+ at binuclear iron ferroxidase centers (FOC) and store the Fe3+ in their interior, thus protecting cells from unwanted Fe3+/Fe2+ redox cycling and storing iron at concentrations far above the solubility of Fe3+. Vertebrate ferritins are heteropolymers of H and L subunits with only the H subunits having FOC. Bfr and Ftn were thought to coexist in bacteria as homopolymers, but recent evidence indicates these molecules are heteropolymers assembled from Bfr and Ftn subunits. Despite the heteropolymeric nature of vertebrate and bacterial ferritins, structures have been determined only for recombinant proteins constituted by a single subunit type. Herein we report the structure of Acinetobacter baumannii bacterioferritin, the first structural example of a heteropolymeric ferritin or ferritin-like molecule, assembled from completely overlapping Ftn homodimers harboring FOC and Bfr homodimers devoid of FOC but binding heme. The Ftn homodimers function by catalyzing the oxidation of Fe2+ to Fe3+, while the Bfr homodimers bind a cognate ferredoxin (Bfd) which reduces the stored Fe3+ by transferring electrons via the heme, enabling Fe2+ mobilization to the cytosol for incorporation in metabolism.
Fil: Yao, Huili. State University of Louisiana; Estados Unidos
Fil: Alli, Suliat. State University of Louisiana; Estados Unidos
Fil: Liu, Lijun. University of Kansas; Estados Unidos
Fil: Soldano, Anabel. State University of Louisiana; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina
Fil: Cooper, Anne. University of Kansas; Estados Unidos
Fil: Fontenot, Leo. State University of Louisiana; Estados Unidos
Fil: Verdin, Dristen. State University of Louisiana; Estados Unidos
Fil: Battaile, Kevin P.. No especifíca;
Fil: Lovell, Scott. University of Kansas; Estados Unidos
Fil: Rivera, Mario. State University of Louisiana; Estados Unidos
Materia
BACTERIOFERRITIN
FERRITIN
IRON METABOLISM
ACINETOBACTER BAUMANNII
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/265389
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/265389
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling The crystal structure of Acinetobacter baumannii bacterioferritin reveals a heteropolymer of bacterioferritin and ferritin subunitsYao, HuiliAlli, SuliatLiu, LijunSoldano, AnabelCooper, AnneFontenot, LeoVerdin, DristenBattaile, Kevin P.Lovell, ScottRivera, MarioBACTERIOFERRITINFERRITINIRON METABOLISMACINETOBACTER BAUMANNIIhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Iron storage proteins, e.g., vertebrate ferritin, and the ferritin-like bacterioferritin (Bfr) and bacterial ferritin (Ftn), are spherical, hollow proteins that catalyze the oxidation of Fe2+ at binuclear iron ferroxidase centers (FOC) and store the Fe3+ in their interior, thus protecting cells from unwanted Fe3+/Fe2+ redox cycling and storing iron at concentrations far above the solubility of Fe3+. Vertebrate ferritins are heteropolymers of H and L subunits with only the H subunits having FOC. Bfr and Ftn were thought to coexist in bacteria as homopolymers, but recent evidence indicates these molecules are heteropolymers assembled from Bfr and Ftn subunits. Despite the heteropolymeric nature of vertebrate and bacterial ferritins, structures have been determined only for recombinant proteins constituted by a single subunit type. Herein we report the structure of Acinetobacter baumannii bacterioferritin, the first structural example of a heteropolymeric ferritin or ferritin-like molecule, assembled from completely overlapping Ftn homodimers harboring FOC and Bfr homodimers devoid of FOC but binding heme. The Ftn homodimers function by catalyzing the oxidation of Fe2+ to Fe3+, while the Bfr homodimers bind a cognate ferredoxin (Bfd) which reduces the stored Fe3+ by transferring electrons via the heme, enabling Fe2+ mobilization to the cytosol for incorporation in metabolism.Fil: Yao, Huili. State University of Louisiana; Estados UnidosFil: Alli, Suliat. State University of Louisiana; Estados UnidosFil: Liu, Lijun. University of Kansas; Estados UnidosFil: Soldano, Anabel. State University of Louisiana; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; ArgentinaFil: Cooper, Anne. University of Kansas; Estados UnidosFil: Fontenot, Leo. State University of Louisiana; Estados UnidosFil: Verdin, Dristen. State University of Louisiana; Estados UnidosFil: Battaile, Kevin P.. No especifíca;Fil: Lovell, Scott. University of Kansas; Estados UnidosFil: Rivera, Mario. State University of Louisiana; Estados UnidosSpringer2024-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/265389Yao, Huili; Alli, Suliat; Liu, Lijun; Soldano, Anabel; Cooper, Anne; et al.; The crystal structure of Acinetobacter baumannii bacterioferritin reveals a heteropolymer of bacterioferritin and ferritin subunits; Springer; Scientific Reports; 14; 1; 8-2024; 1-142045-2322CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.nature.com/articles/s41598-024-69156-2info:eu-repo/semantics/altIdentifier/doi/10.1038/s41598-024-69156-2info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:15:21Zoai:ri.conicet.gov.ar:11336/265389instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:15:21.928CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The crystal structure of Acinetobacter baumannii bacterioferritin reveals a heteropolymer of bacterioferritin and ferritin subunits
title The crystal structure of Acinetobacter baumannii bacterioferritin reveals a heteropolymer of bacterioferritin and ferritin subunits
spellingShingle The crystal structure of Acinetobacter baumannii bacterioferritin reveals a heteropolymer of bacterioferritin and ferritin subunits
Yao, Huili
BACTERIOFERRITIN
FERRITIN
IRON METABOLISM
ACINETOBACTER BAUMANNII
title_short The crystal structure of Acinetobacter baumannii bacterioferritin reveals a heteropolymer of bacterioferritin and ferritin subunits
title_full The crystal structure of Acinetobacter baumannii bacterioferritin reveals a heteropolymer of bacterioferritin and ferritin subunits
title_fullStr The crystal structure of Acinetobacter baumannii bacterioferritin reveals a heteropolymer of bacterioferritin and ferritin subunits
title_full_unstemmed The crystal structure of Acinetobacter baumannii bacterioferritin reveals a heteropolymer of bacterioferritin and ferritin subunits
title_sort The crystal structure of Acinetobacter baumannii bacterioferritin reveals a heteropolymer of bacterioferritin and ferritin subunits
dc.creator.none.fl_str_mv Yao, Huili
Alli, Suliat
Liu, Lijun
Soldano, Anabel
Cooper, Anne
Fontenot, Leo
Verdin, Dristen
Battaile, Kevin P.
Lovell, Scott
Rivera, Mario
author Yao, Huili
author_facet Yao, Huili
Alli, Suliat
Liu, Lijun
Soldano, Anabel
Cooper, Anne
Fontenot, Leo
Verdin, Dristen
Battaile, Kevin P.
Lovell, Scott
Rivera, Mario
author_role author
author2 Alli, Suliat
Liu, Lijun
Soldano, Anabel
Cooper, Anne
Fontenot, Leo
Verdin, Dristen
Battaile, Kevin P.
Lovell, Scott
Rivera, Mario
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv BACTERIOFERRITIN
FERRITIN
IRON METABOLISM
ACINETOBACTER BAUMANNII
topic BACTERIOFERRITIN
FERRITIN
IRON METABOLISM
ACINETOBACTER BAUMANNII
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Iron storage proteins, e.g., vertebrate ferritin, and the ferritin-like bacterioferritin (Bfr) and bacterial ferritin (Ftn), are spherical, hollow proteins that catalyze the oxidation of Fe2+ at binuclear iron ferroxidase centers (FOC) and store the Fe3+ in their interior, thus protecting cells from unwanted Fe3+/Fe2+ redox cycling and storing iron at concentrations far above the solubility of Fe3+. Vertebrate ferritins are heteropolymers of H and L subunits with only the H subunits having FOC. Bfr and Ftn were thought to coexist in bacteria as homopolymers, but recent evidence indicates these molecules are heteropolymers assembled from Bfr and Ftn subunits. Despite the heteropolymeric nature of vertebrate and bacterial ferritins, structures have been determined only for recombinant proteins constituted by a single subunit type. Herein we report the structure of Acinetobacter baumannii bacterioferritin, the first structural example of a heteropolymeric ferritin or ferritin-like molecule, assembled from completely overlapping Ftn homodimers harboring FOC and Bfr homodimers devoid of FOC but binding heme. The Ftn homodimers function by catalyzing the oxidation of Fe2+ to Fe3+, while the Bfr homodimers bind a cognate ferredoxin (Bfd) which reduces the stored Fe3+ by transferring electrons via the heme, enabling Fe2+ mobilization to the cytosol for incorporation in metabolism.
Fil: Yao, Huili. State University of Louisiana; Estados Unidos
Fil: Alli, Suliat. State University of Louisiana; Estados Unidos
Fil: Liu, Lijun. University of Kansas; Estados Unidos
Fil: Soldano, Anabel. State University of Louisiana; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina
Fil: Cooper, Anne. University of Kansas; Estados Unidos
Fil: Fontenot, Leo. State University of Louisiana; Estados Unidos
Fil: Verdin, Dristen. State University of Louisiana; Estados Unidos
Fil: Battaile, Kevin P.. No especifíca;
Fil: Lovell, Scott. University of Kansas; Estados Unidos
Fil: Rivera, Mario. State University of Louisiana; Estados Unidos
description Iron storage proteins, e.g., vertebrate ferritin, and the ferritin-like bacterioferritin (Bfr) and bacterial ferritin (Ftn), are spherical, hollow proteins that catalyze the oxidation of Fe2+ at binuclear iron ferroxidase centers (FOC) and store the Fe3+ in their interior, thus protecting cells from unwanted Fe3+/Fe2+ redox cycling and storing iron at concentrations far above the solubility of Fe3+. Vertebrate ferritins are heteropolymers of H and L subunits with only the H subunits having FOC. Bfr and Ftn were thought to coexist in bacteria as homopolymers, but recent evidence indicates these molecules are heteropolymers assembled from Bfr and Ftn subunits. Despite the heteropolymeric nature of vertebrate and bacterial ferritins, structures have been determined only for recombinant proteins constituted by a single subunit type. Herein we report the structure of Acinetobacter baumannii bacterioferritin, the first structural example of a heteropolymeric ferritin or ferritin-like molecule, assembled from completely overlapping Ftn homodimers harboring FOC and Bfr homodimers devoid of FOC but binding heme. The Ftn homodimers function by catalyzing the oxidation of Fe2+ to Fe3+, while the Bfr homodimers bind a cognate ferredoxin (Bfd) which reduces the stored Fe3+ by transferring electrons via the heme, enabling Fe2+ mobilization to the cytosol for incorporation in metabolism.
publishDate 2024
dc.date.none.fl_str_mv 2024-08
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/265389
Yao, Huili; Alli, Suliat; Liu, Lijun; Soldano, Anabel; Cooper, Anne; et al.; The crystal structure of Acinetobacter baumannii bacterioferritin reveals a heteropolymer of bacterioferritin and ferritin subunits; Springer; Scientific Reports; 14; 1; 8-2024; 1-14
2045-2322
CONICET Digital
CONICET
url http://hdl.handle.net/11336/265389
identifier_str_mv Yao, Huili; Alli, Suliat; Liu, Lijun; Soldano, Anabel; Cooper, Anne; et al.; The crystal structure of Acinetobacter baumannii bacterioferritin reveals a heteropolymer of bacterioferritin and ferritin subunits; Springer; Scientific Reports; 14; 1; 8-2024; 1-14
2045-2322
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.nature.com/articles/s41598-024-69156-2
info:eu-repo/semantics/altIdentifier/doi/10.1038/s41598-024-69156-2
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Springer
publisher.none.fl_str_mv Springer
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.069144

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