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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/8811
Ver los metadatos del registro completo
id |
CONICETDig_bc438fd3ee7e91f9f98941e12859ab71 |
---|---|
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 Técnicas2025-09-29T10:40:41Zoai: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:34982025-09-29 10:40:41.459CONICET 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 |
_version_ |
1844614435778330624 |
score |
13.070432 |