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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/268734
Ver los metadatos del registro completo
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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 Técnicas2025-09-29T10:24:59Zoai: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:34982025-09-29 10:24:59.286CONICET 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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1844614247492878336 |
score |
13.070432 |