A tetrahedral coordination of Zinc during transmembrane transport by P-type Zn2+-ATPases

Autores
Raimunda, Daniel Cesar; Subramanian, Poorna; Stemmler, Timothy; Argüello, José M.
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Zn2 + is an essential transition metal required in trace amounts by all living organisms. However, metal excess is cytotoxic and leads to cell damage. Cells rely on transmembrane transporters, with the assistance of other proteins, to establish and maintain Zn2 + homeostasis. Metal coordination during transport is key to specific transport and unidirectional translocation without the backward release of free metal. The coordination details of Zn2 + at the transmembrane metal binding site responsible for transport have now been established. Escherichia coli ZntA is a well-characterized Zn2 +-ATPase responsible for intracellular Zn2 + efflux. A truncated form of the protein lacking regulatory metal sites and retaining the transport site was constructed. Metrical parameters of the metal-ligand coordination geometry for the zinc bound isolated form were characterized using x-ray absorption spectroscopy (XAS). Our data support a nearest neighbor ligand environment of (O/N)2S2 that is compatible with the proposed invariant metal coordinating residues present in the transmembrane region. This ligand identification and the calculated bond lengths support a tetrahedral coordination geometry for Zn2 + bound to the TM-MBS of P-type ATPase transporters.
Fil: Raimunda, Daniel Cesar. Worcester Polytechnic Institute. Departmen Of Chemistry And Biochemistry; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina
Fil: Subramanian, Poorna. Wayne State University; Estados Unidos
Fil: Stemmler, Timothy. Wayne State University; Estados Unidos
Fil: Argüello, José M.. Worcester Polytechnic Institute. Departmen Of Chemistry And Biochemistry; Estados Unidos
Materia
Zinc
Transport
Metal coordination
EXAFS
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/268734
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/268734
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling A tetrahedral coordination of Zinc during transmembrane transport by P-type Zn2+-ATPasesRaimunda, Daniel CesarSubramanian, PoornaStemmler, TimothyArgüello, José M.ZincTransportMetal coordinationEXAFShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Zn2 + is an essential transition metal required in trace amounts by all living organisms. However, metal excess is cytotoxic and leads to cell damage. Cells rely on transmembrane transporters, with the assistance of other proteins, to establish and maintain Zn2 + homeostasis. Metal coordination during transport is key to specific transport and unidirectional translocation without the backward release of free metal. The coordination details of Zn2 + at the transmembrane metal binding site responsible for transport have now been established. Escherichia coli ZntA is a well-characterized Zn2 +-ATPase responsible for intracellular Zn2 + efflux. A truncated form of the protein lacking regulatory metal sites and retaining the transport site was constructed. Metrical parameters of the metal-ligand coordination geometry for the zinc bound isolated form were characterized using x-ray absorption spectroscopy (XAS). Our data support a nearest neighbor ligand environment of (O/N)2S2 that is compatible with the proposed invariant metal coordinating residues present in the transmembrane region. This ligand identification and the calculated bond lengths support a tetrahedral coordination geometry for Zn2 + bound to the TM-MBS of P-type ATPase transporters.Fil: Raimunda, Daniel Cesar. Worcester Polytechnic Institute. Departmen Of Chemistry And Biochemistry; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; ArgentinaFil: Subramanian, Poorna. Wayne State University; Estados UnidosFil: Stemmler, Timothy. Wayne State University; Estados UnidosFil: Argüello, José M.. Worcester Polytechnic Institute. Departmen Of Chemistry And Biochemistry; Estados UnidosElsevier Science2012-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/268734Raimunda, Daniel Cesar; Subramanian, Poorna; Stemmler, Timothy; Argüello, José M.; A tetrahedral coordination of Zinc during transmembrane transport by P-type Zn2+-ATPases; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1818; 5; 5-2012; 1374-13770005-2736CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0005273612000715info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2012.02.020info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:57:43Zoai:ri.conicet.gov.ar:11336/268734instacron: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:34982025-10-22 11:57:43.307CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A tetrahedral coordination of Zinc during transmembrane transport by P-type Zn2+-ATPases
title A tetrahedral coordination of Zinc during transmembrane transport by P-type Zn2+-ATPases
spellingShingle A tetrahedral coordination of Zinc during transmembrane transport by P-type Zn2+-ATPases
Raimunda, Daniel Cesar
Zinc
Transport
Metal coordination
EXAFS
title_short A tetrahedral coordination of Zinc during transmembrane transport by P-type Zn2+-ATPases
title_full A tetrahedral coordination of Zinc during transmembrane transport by P-type Zn2+-ATPases
title_fullStr A tetrahedral coordination of Zinc during transmembrane transport by P-type Zn2+-ATPases
title_full_unstemmed A tetrahedral coordination of Zinc during transmembrane transport by P-type Zn2+-ATPases
title_sort A tetrahedral coordination of Zinc during transmembrane transport by P-type Zn2+-ATPases
dc.creator.none.fl_str_mv Raimunda, Daniel Cesar
Subramanian, Poorna
Stemmler, Timothy
Argüello, José M.
author Raimunda, Daniel Cesar
author_facet Raimunda, Daniel Cesar
Subramanian, Poorna
Stemmler, Timothy
Argüello, José M.
author_role author
author2 Subramanian, Poorna
Stemmler, Timothy
Argüello, José M.
author2_role author
author
author
dc.subject.none.fl_str_mv Zinc
Transport
Metal coordination
EXAFS
topic Zinc
Transport
Metal coordination
EXAFS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Zn2 + is an essential transition metal required in trace amounts by all living organisms. However, metal excess is cytotoxic and leads to cell damage. Cells rely on transmembrane transporters, with the assistance of other proteins, to establish and maintain Zn2 + homeostasis. Metal coordination during transport is key to specific transport and unidirectional translocation without the backward release of free metal. The coordination details of Zn2 + at the transmembrane metal binding site responsible for transport have now been established. Escherichia coli ZntA is a well-characterized Zn2 +-ATPase responsible for intracellular Zn2 + efflux. A truncated form of the protein lacking regulatory metal sites and retaining the transport site was constructed. Metrical parameters of the metal-ligand coordination geometry for the zinc bound isolated form were characterized using x-ray absorption spectroscopy (XAS). Our data support a nearest neighbor ligand environment of (O/N)2S2 that is compatible with the proposed invariant metal coordinating residues present in the transmembrane region. This ligand identification and the calculated bond lengths support a tetrahedral coordination geometry for Zn2 + bound to the TM-MBS of P-type ATPase transporters.
Fil: Raimunda, Daniel Cesar. Worcester Polytechnic Institute. Departmen Of Chemistry And Biochemistry; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra. Universidad Nacional de Córdoba. Instituto de Investigación Médica Mercedes y Martín Ferreyra; Argentina
Fil: Subramanian, Poorna. Wayne State University; Estados Unidos
Fil: Stemmler, Timothy. Wayne State University; Estados Unidos
Fil: Argüello, José M.. Worcester Polytechnic Institute. Departmen Of Chemistry And Biochemistry; Estados Unidos
description Zn2 + is an essential transition metal required in trace amounts by all living organisms. However, metal excess is cytotoxic and leads to cell damage. Cells rely on transmembrane transporters, with the assistance of other proteins, to establish and maintain Zn2 + homeostasis. Metal coordination during transport is key to specific transport and unidirectional translocation without the backward release of free metal. The coordination details of Zn2 + at the transmembrane metal binding site responsible for transport have now been established. Escherichia coli ZntA is a well-characterized Zn2 +-ATPase responsible for intracellular Zn2 + efflux. A truncated form of the protein lacking regulatory metal sites and retaining the transport site was constructed. Metrical parameters of the metal-ligand coordination geometry for the zinc bound isolated form were characterized using x-ray absorption spectroscopy (XAS). Our data support a nearest neighbor ligand environment of (O/N)2S2 that is compatible with the proposed invariant metal coordinating residues present in the transmembrane region. This ligand identification and the calculated bond lengths support a tetrahedral coordination geometry for Zn2 + bound to the TM-MBS of P-type ATPase transporters.
publishDate 2012
dc.date.none.fl_str_mv 2012-05
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/11336/268734
Raimunda, Daniel Cesar; Subramanian, Poorna; Stemmler, Timothy; Argüello, José M.; A tetrahedral coordination of Zinc during transmembrane transport by P-type Zn2+-ATPases; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1818; 5; 5-2012; 1374-1377
0005-2736
CONICET Digital
CONICET
url http://hdl.handle.net/11336/268734
identifier_str_mv Raimunda, Daniel Cesar; Subramanian, Poorna; Stemmler, Timothy; Argüello, José M.; A tetrahedral coordination of Zinc during transmembrane transport by P-type Zn2+-ATPases; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1818; 5; 5-2012; 1374-1377
0005-2736
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.sciencedirect.com/science/article/pii/S0005273612000715
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2012.02.020
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
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 12.982451

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