A dimerization interface mediated by functionally critical residues creates interfacial disulfide bonds and copper sites in CueP

Autores
Abriata, Luciano Andres; Pontel, Lucas Blas; Vila, Alejandro Jose; Dal Peraro, Matteo; Soncini, Fernando Carlos
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
CueP confers bacterial copper resistance in the periplasm, particularly under anaerobic conditions, through an unknown mechanism. The only available structure and limited solution data suggest that CueP forms noncovalent dimers in solution, whereas sequence conservation suggests important roles for three cysteines and two histidines as copper ligands. Here we report evidence of a dimerization equilibrium mediated by a newly identified interface of functional relevance, which occludes internal copper sites and disulfide bonds but allows for intra- and interchain disulfide bonding, an extensive disulfide relay, and interfacial copper sites. Our results suggest a role for CueP linking redox-state sensing and copper detoxification.
Fil: Abriata, Luciano Andres. Swiss Institute Of Bioinformatics, Lausanne; Suiza
Fil: Pontel, Lucas Blas. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Vila, Alejandro Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Dal Peraro, Matteo. Swiss Institute Of Bioinformatics, Lausanne; Suiza
Fil: Soncini, Fernando Carlos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; Argentina
Materia
Copper Tolerance And Homeostasis
Disulfide Relay
Periplasm
Salmonella Enterica
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:11336/8811
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/8811
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling A dimerization interface mediated by functionally critical residues creates interfacial disulfide bonds and copper sites in CuePAbriata, Luciano AndresPontel, Lucas BlasVila, Alejandro JoseDal Peraro, MatteoSoncini, Fernando CarlosCopper Tolerance And HomeostasisDisulfide RelayPeriplasmSalmonella Entericahttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1CueP confers bacterial copper resistance in the periplasm, particularly under anaerobic conditions, through an unknown mechanism. The only available structure and limited solution data suggest that CueP forms noncovalent dimers in solution, whereas sequence conservation suggests important roles for three cysteines and two histidines as copper ligands. Here we report evidence of a dimerization equilibrium mediated by a newly identified interface of functional relevance, which occludes internal copper sites and disulfide bonds but allows for intra- and interchain disulfide bonding, an extensive disulfide relay, and interfacial copper sites. Our results suggest a role for CueP linking redox-state sensing and copper detoxification.Fil: Abriata, Luciano Andres. Swiss Institute Of Bioinformatics, Lausanne; SuizaFil: Pontel, Lucas Blas. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Vila, Alejandro Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; ArgentinaFil: Dal Peraro, Matteo. Swiss Institute Of Bioinformatics, Lausanne; SuizaFil: Soncini, Fernando Carlos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; ArgentinaElsevier2014-08info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/8811Abriata, Luciano Andres; Pontel, Lucas Blas; Vila, Alejandro Jose; Dal Peraro, Matteo; Soncini, Fernando Carlos; A dimerization interface mediated by functionally critical residues creates interfacial disulfide bonds and copper sites in CueP; Elsevier; Journal Of Inorganic Biochemistry; 140; 8-2014; 199-2010162-0134enginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.jinorgbio.2014.07.022info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0162013414002190info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:38:31Zoai:ri.conicet.gov.ar:11336/8811instacron: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:34982025-10-15 15:38:31.319CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv A dimerization interface mediated by functionally critical residues creates interfacial disulfide bonds and copper sites in CueP
title A dimerization interface mediated by functionally critical residues creates interfacial disulfide bonds and copper sites in CueP
spellingShingle A dimerization interface mediated by functionally critical residues creates interfacial disulfide bonds and copper sites in CueP
Abriata, Luciano Andres
Copper Tolerance And Homeostasis
Disulfide Relay
Periplasm
Salmonella Enterica
title_short A dimerization interface mediated by functionally critical residues creates interfacial disulfide bonds and copper sites in CueP
title_full A dimerization interface mediated by functionally critical residues creates interfacial disulfide bonds and copper sites in CueP
title_fullStr A dimerization interface mediated by functionally critical residues creates interfacial disulfide bonds and copper sites in CueP
title_full_unstemmed A dimerization interface mediated by functionally critical residues creates interfacial disulfide bonds and copper sites in CueP
title_sort A dimerization interface mediated by functionally critical residues creates interfacial disulfide bonds and copper sites in CueP
dc.creator.none.fl_str_mv Abriata, Luciano Andres
Pontel, Lucas Blas
Vila, Alejandro Jose
Dal Peraro, Matteo
Soncini, Fernando Carlos
author Abriata, Luciano Andres
author_facet Abriata, Luciano Andres
Pontel, Lucas Blas
Vila, Alejandro Jose
Dal Peraro, Matteo
Soncini, Fernando Carlos
author_role author
author2 Pontel, Lucas Blas
Vila, Alejandro Jose
Dal Peraro, Matteo
Soncini, Fernando Carlos
author2_role author
author
author
author
dc.subject.none.fl_str_mv Copper Tolerance And Homeostasis
Disulfide Relay
Periplasm
Salmonella Enterica
topic Copper Tolerance And Homeostasis
Disulfide Relay
Periplasm
Salmonella Enterica
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv CueP confers bacterial copper resistance in the periplasm, particularly under anaerobic conditions, through an unknown mechanism. The only available structure and limited solution data suggest that CueP forms noncovalent dimers in solution, whereas sequence conservation suggests important roles for three cysteines and two histidines as copper ligands. Here we report evidence of a dimerization equilibrium mediated by a newly identified interface of functional relevance, which occludes internal copper sites and disulfide bonds but allows for intra- and interchain disulfide bonding, an extensive disulfide relay, and interfacial copper sites. Our results suggest a role for CueP linking redox-state sensing and copper detoxification.
Fil: Abriata, Luciano Andres. Swiss Institute Of Bioinformatics, Lausanne; Suiza
Fil: Pontel, Lucas Blas. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Vila, Alejandro Jose. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; Argentina
Fil: Dal Peraro, Matteo. Swiss Institute Of Bioinformatics, Lausanne; Suiza
Fil: Soncini, Fernando Carlos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Rosario. Instituto de Biología Molecular y Celular de Rosario; Argentina
description CueP confers bacterial copper resistance in the periplasm, particularly under anaerobic conditions, through an unknown mechanism. The only available structure and limited solution data suggest that CueP forms noncovalent dimers in solution, whereas sequence conservation suggests important roles for three cysteines and two histidines as copper ligands. Here we report evidence of a dimerization equilibrium mediated by a newly identified interface of functional relevance, which occludes internal copper sites and disulfide bonds but allows for intra- and interchain disulfide bonding, an extensive disulfide relay, and interfacial copper sites. Our results suggest a role for CueP linking redox-state sensing and copper detoxification.
publishDate 2014
dc.date.none.fl_str_mv 2014-08
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/11336/8811
Abriata, Luciano Andres; Pontel, Lucas Blas; Vila, Alejandro Jose; Dal Peraro, Matteo; Soncini, Fernando Carlos; A dimerization interface mediated by functionally critical residues creates interfacial disulfide bonds and copper sites in CueP; Elsevier; Journal Of Inorganic Biochemistry; 140; 8-2014; 199-201
0162-0134
url http://hdl.handle.net/11336/8811
identifier_str_mv Abriata, Luciano Andres; Pontel, Lucas Blas; Vila, Alejandro Jose; Dal Peraro, Matteo; Soncini, Fernando Carlos; A dimerization interface mediated by functionally critical residues creates interfacial disulfide bonds and copper sites in CueP; Elsevier; Journal Of Inorganic Biochemistry; 140; 8-2014; 199-201
0162-0134
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jinorgbio.2014.07.022
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0162013414002190
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
application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
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 13.22299

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