Putative binding mode of Escherichia coli exopolyphosphatase and polyphosphates based on a hybrid in silico/biochemical approach

Autores
Boetsch, Cristhian; Aguayo Villegas, Daniel R.; Gonzalez Nilo, Fernando Danilo; Lisa, Angela Teresita; Beassoni, Paola Rita
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The exopolyphosphatase of Escherichia coli processively and completely hydrolyses long polyphosphate chains to ortho-phosphate. Genetic surveys, based on the analysis of single ppx− or ppk− mutants and on the double mutant, demonstrate a relationship between these genes and the survival capacity. The exopolyphosphatase belongs to the ASKHA protein superfamily, hence, its active site is well known; however, the knowledge of the way in which this enzyme binds polyP remains incomplete. Here we present different computational approaches, site-direct mutagenesis and kinetic data to understand the relationship between structure and function of exopolyphosphatase. We propose H378 as a fundamental gatekeeper for the recognition of long chain polyphosphate.
Fil: Boetsch, Cristhian. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Biología Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina
Fil: Aguayo Villegas, Daniel R.. Universidad Andres Bello. Centro de Bioinformatica y Biología Integrativa; Chile
Fil: Gonzalez Nilo, Fernando Danilo. Universidad Andres Bello. Centro de Bioinformatica y Biología Integrativa; Chile
Fil: Lisa, Angela Teresita. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Biología Molecular; Argentina
Fil: Beassoni, Paola Rita. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Biología Molecular; Argentina
Materia
BINDING
EXOPOLYPHOSPHATASE
MOLECULAR DYNAMICS
POLYPHOSPHATE
PROCESSIVITY
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:11336/179979
Acceder
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repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Putative binding mode of Escherichia coli exopolyphosphatase and polyphosphates based on a hybrid in silico/biochemical approachBoetsch, CristhianAguayo Villegas, Daniel R.Gonzalez Nilo, Fernando DaniloLisa, Angela TeresitaBeassoni, Paola RitaBINDINGEXOPOLYPHOSPHATASEMOLECULAR DYNAMICSPOLYPHOSPHATEPROCESSIVITYhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The exopolyphosphatase of Escherichia coli processively and completely hydrolyses long polyphosphate chains to ortho-phosphate. Genetic surveys, based on the analysis of single ppx− or ppk− mutants and on the double mutant, demonstrate a relationship between these genes and the survival capacity. The exopolyphosphatase belongs to the ASKHA protein superfamily, hence, its active site is well known; however, the knowledge of the way in which this enzyme binds polyP remains incomplete. Here we present different computational approaches, site-direct mutagenesis and kinetic data to understand the relationship between structure and function of exopolyphosphatase. We propose H378 as a fundamental gatekeeper for the recognition of long chain polyphosphate.Fil: Boetsch, Cristhian. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Biología Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; ArgentinaFil: Aguayo Villegas, Daniel R.. Universidad Andres Bello. Centro de Bioinformatica y Biología Integrativa; ChileFil: Gonzalez Nilo, Fernando Danilo. Universidad Andres Bello. Centro de Bioinformatica y Biología Integrativa; ChileFil: Lisa, Angela Teresita. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Biología Molecular; ArgentinaFil: Beassoni, Paola Rita. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Biología Molecular; ArgentinaElsevier Science Inc.2016-07info: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/11336/179979Boetsch, Cristhian; Aguayo Villegas, Daniel R.; Gonzalez Nilo, Fernando Danilo; Lisa, Angela Teresita; Beassoni, Paola Rita; Putative binding mode of Escherichia coli exopolyphosphatase and polyphosphates based on a hybrid in silico/biochemical approach; Elsevier Science Inc.; Archives of Biochemistry and Biophysics; 606; 7-2016; 64-720003-9861CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/abs/pii/S0003986116302235?via%3Dihubinfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.abb.2016.07.005info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:53:01Zoai:ri.conicet.gov.ar:11336/179979instacron: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:34982025-09-03 09:53:01.787CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Putative binding mode of Escherichia coli exopolyphosphatase and polyphosphates based on a hybrid in silico/biochemical approach
title Putative binding mode of Escherichia coli exopolyphosphatase and polyphosphates based on a hybrid in silico/biochemical approach
spellingShingle Putative binding mode of Escherichia coli exopolyphosphatase and polyphosphates based on a hybrid in silico/biochemical approach
Boetsch, Cristhian
BINDING
EXOPOLYPHOSPHATASE
MOLECULAR DYNAMICS
POLYPHOSPHATE
PROCESSIVITY
title_short Putative binding mode of Escherichia coli exopolyphosphatase and polyphosphates based on a hybrid in silico/biochemical approach
title_full Putative binding mode of Escherichia coli exopolyphosphatase and polyphosphates based on a hybrid in silico/biochemical approach
title_fullStr Putative binding mode of Escherichia coli exopolyphosphatase and polyphosphates based on a hybrid in silico/biochemical approach
title_full_unstemmed Putative binding mode of Escherichia coli exopolyphosphatase and polyphosphates based on a hybrid in silico/biochemical approach
title_sort Putative binding mode of Escherichia coli exopolyphosphatase and polyphosphates based on a hybrid in silico/biochemical approach
dc.creator.none.fl_str_mv Boetsch, Cristhian
Aguayo Villegas, Daniel R.
Gonzalez Nilo, Fernando Danilo
Lisa, Angela Teresita
Beassoni, Paola Rita
author Boetsch, Cristhian
author_facet Boetsch, Cristhian
Aguayo Villegas, Daniel R.
Gonzalez Nilo, Fernando Danilo
Lisa, Angela Teresita
Beassoni, Paola Rita
author_role author
author2 Aguayo Villegas, Daniel R.
Gonzalez Nilo, Fernando Danilo
Lisa, Angela Teresita
Beassoni, Paola Rita
author2_role author
author
author
author
dc.subject.none.fl_str_mv BINDING
EXOPOLYPHOSPHATASE
MOLECULAR DYNAMICS
POLYPHOSPHATE
PROCESSIVITY
topic BINDING
EXOPOLYPHOSPHATASE
MOLECULAR DYNAMICS
POLYPHOSPHATE
PROCESSIVITY
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv The exopolyphosphatase of Escherichia coli processively and completely hydrolyses long polyphosphate chains to ortho-phosphate. Genetic surveys, based on the analysis of single ppx− or ppk− mutants and on the double mutant, demonstrate a relationship between these genes and the survival capacity. The exopolyphosphatase belongs to the ASKHA protein superfamily, hence, its active site is well known; however, the knowledge of the way in which this enzyme binds polyP remains incomplete. Here we present different computational approaches, site-direct mutagenesis and kinetic data to understand the relationship between structure and function of exopolyphosphatase. We propose H378 as a fundamental gatekeeper for the recognition of long chain polyphosphate.
Fil: Boetsch, Cristhian. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Biología Molecular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina
Fil: Aguayo Villegas, Daniel R.. Universidad Andres Bello. Centro de Bioinformatica y Biología Integrativa; Chile
Fil: Gonzalez Nilo, Fernando Danilo. Universidad Andres Bello. Centro de Bioinformatica y Biología Integrativa; Chile
Fil: Lisa, Angela Teresita. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Biología Molecular; Argentina
Fil: Beassoni, Paola Rita. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba; Argentina. Universidad Nacional de Río Cuarto. Facultad de Ciencias Exactas Fisicoquímicas y Naturales. Departamento de Biología Molecular; Argentina
description The exopolyphosphatase of Escherichia coli processively and completely hydrolyses long polyphosphate chains to ortho-phosphate. Genetic surveys, based on the analysis of single ppx− or ppk− mutants and on the double mutant, demonstrate a relationship between these genes and the survival capacity. The exopolyphosphatase belongs to the ASKHA protein superfamily, hence, its active site is well known; however, the knowledge of the way in which this enzyme binds polyP remains incomplete. Here we present different computational approaches, site-direct mutagenesis and kinetic data to understand the relationship between structure and function of exopolyphosphatase. We propose H378 as a fundamental gatekeeper for the recognition of long chain polyphosphate.
publishDate 2016
dc.date.none.fl_str_mv 2016-07
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/11336/179979
Boetsch, Cristhian; Aguayo Villegas, Daniel R.; Gonzalez Nilo, Fernando Danilo; Lisa, Angela Teresita; Beassoni, Paola Rita; Putative binding mode of Escherichia coli exopolyphosphatase and polyphosphates based on a hybrid in silico/biochemical approach; Elsevier Science Inc.; Archives of Biochemistry and Biophysics; 606; 7-2016; 64-72
0003-9861
CONICET Digital
CONICET
url http://hdl.handle.net/11336/179979
identifier_str_mv Boetsch, Cristhian; Aguayo Villegas, Daniel R.; Gonzalez Nilo, Fernando Danilo; Lisa, Angela Teresita; Beassoni, Paola Rita; Putative binding mode of Escherichia coli exopolyphosphatase and polyphosphates based on a hybrid in silico/biochemical approach; Elsevier Science Inc.; Archives of Biochemistry and Biophysics; 606; 7-2016; 64-72
0003-9861
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/abs/pii/S0003986116302235?via%3Dihub
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.abb.2016.07.005
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 Science Inc.
publisher.none.fl_str_mv Elsevier Science Inc.
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_ 1842269196212240384
score 13.13397

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