The structure of Synechococcus elongatus enolase reveals key aspects of phosphoenolpyruvate binding

Autores
Gonzalez, Javier Marcelo; Martí Arbona, Ricardo; Chen, Julian C. H.; Unkefer, Clifford
Año de publicación
2022
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
A structure-function characterization of Synechococcus elongatus enolase (SeEN) is presented, representing the first structural report on a cyanobacterial enolase. X-ray crystal structures of SeEN in its apoenzyme form and in complex with phosphoenolpyruvate are reported at 2.05 and 2.30 Å resolution, respectively. SeEN displays the typical fold of enolases, with a conformationally flexible loop that closes the active site upon substrate binding, assisted by two metal ions that stabilize the negatively charged groups. The enzyme exhibits a catalytic efficiency of 1.2 × 105 M -1s-1for the dehydration of 2-phospho-d-glycerate, which is comparable to the kinetic parameters of related enzymes. These results expand the understanding of the biophysical features of these enzymes, broadening the toolbox for metabolic engineering applications.
Fil: Gonzalez, Javier Marcelo. Universidad Nacional de Santiago del Estero. Instituto de Bionanotecnología del Noa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Bionanotecnología del Noa; Argentina
Fil: Martí Arbona, Ricardo. Los Alamos National High Magnetic Field Laboratory; Estados Unidos
Fil: Chen, Julian C. H.. Los Alamos National High Magnetic Field Laboratory; Estados Unidos
Fil: Unkefer, Clifford. Los Alamos National High Magnetic Field Laboratory; Estados Unidos
Materia
CYANOBACTERIA
ENOLASES
PHOSPHOENOLPYRUVATE
SYNECHOCOCCUS ELONGATUS
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:11336/213746
Acceder
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network_name_str CONICET Digital (CONICET)
spelling The structure of Synechococcus elongatus enolase reveals key aspects of phosphoenolpyruvate bindingGonzalez, Javier MarceloMartí Arbona, RicardoChen, Julian C. H.Unkefer, CliffordCYANOBACTERIAENOLASESPHOSPHOENOLPYRUVATESYNECHOCOCCUS ELONGATUShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1A structure-function characterization of Synechococcus elongatus enolase (SeEN) is presented, representing the first structural report on a cyanobacterial enolase. X-ray crystal structures of SeEN in its apoenzyme form and in complex with phosphoenolpyruvate are reported at 2.05 and 2.30 Å resolution, respectively. SeEN displays the typical fold of enolases, with a conformationally flexible loop that closes the active site upon substrate binding, assisted by two metal ions that stabilize the negatively charged groups. The enzyme exhibits a catalytic efficiency of 1.2 × 105 M -1s-1for the dehydration of 2-phospho-d-glycerate, which is comparable to the kinetic parameters of related enzymes. These results expand the understanding of the biophysical features of these enzymes, broadening the toolbox for metabolic engineering applications.Fil: Gonzalez, Javier Marcelo. Universidad Nacional de Santiago del Estero. Instituto de Bionanotecnología del Noa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Bionanotecnología del Noa; ArgentinaFil: Martí Arbona, Ricardo. Los Alamos National High Magnetic Field Laboratory; Estados UnidosFil: Chen, Julian C. H.. Los Alamos National High Magnetic Field Laboratory; Estados UnidosFil: Unkefer, Clifford. Los Alamos National High Magnetic Field Laboratory; Estados UnidosWiley Blackwell Publishing, Inc2022-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/213746Gonzalez, Javier Marcelo; Martí Arbona, Ricardo; Chen, Julian C. H.; Unkefer, Clifford; The structure of Synechococcus elongatus enolase reveals key aspects of phosphoenolpyruvate binding; Wiley Blackwell Publishing, Inc; Acta Crystallographica Section F: Structural Biology Communications; 78; 4-2022; 177-1842053-230XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://scripts.iucr.org/cgi-bin/paper?S2053230X22003612info:eu-repo/semantics/altIdentifier/doi/10.1107/S2053230X22003612info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:05:33Zoai:ri.conicet.gov.ar:11336/213746instacron: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 10:05:33.44CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The structure of Synechococcus elongatus enolase reveals key aspects of phosphoenolpyruvate binding
title The structure of Synechococcus elongatus enolase reveals key aspects of phosphoenolpyruvate binding
spellingShingle The structure of Synechococcus elongatus enolase reveals key aspects of phosphoenolpyruvate binding
Gonzalez, Javier Marcelo
CYANOBACTERIA
ENOLASES
PHOSPHOENOLPYRUVATE
SYNECHOCOCCUS ELONGATUS
title_short The structure of Synechococcus elongatus enolase reveals key aspects of phosphoenolpyruvate binding
title_full The structure of Synechococcus elongatus enolase reveals key aspects of phosphoenolpyruvate binding
title_fullStr The structure of Synechococcus elongatus enolase reveals key aspects of phosphoenolpyruvate binding
title_full_unstemmed The structure of Synechococcus elongatus enolase reveals key aspects of phosphoenolpyruvate binding
title_sort The structure of Synechococcus elongatus enolase reveals key aspects of phosphoenolpyruvate binding
dc.creator.none.fl_str_mv Gonzalez, Javier Marcelo
Martí Arbona, Ricardo
Chen, Julian C. H.
Unkefer, Clifford
author Gonzalez, Javier Marcelo
author_facet Gonzalez, Javier Marcelo
Martí Arbona, Ricardo
Chen, Julian C. H.
Unkefer, Clifford
author_role author
author2 Martí Arbona, Ricardo
Chen, Julian C. H.
Unkefer, Clifford
author2_role author
author
author
dc.subject.none.fl_str_mv CYANOBACTERIA
ENOLASES
PHOSPHOENOLPYRUVATE
SYNECHOCOCCUS ELONGATUS
topic CYANOBACTERIA
ENOLASES
PHOSPHOENOLPYRUVATE
SYNECHOCOCCUS ELONGATUS
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv A structure-function characterization of Synechococcus elongatus enolase (SeEN) is presented, representing the first structural report on a cyanobacterial enolase. X-ray crystal structures of SeEN in its apoenzyme form and in complex with phosphoenolpyruvate are reported at 2.05 and 2.30 Å resolution, respectively. SeEN displays the typical fold of enolases, with a conformationally flexible loop that closes the active site upon substrate binding, assisted by two metal ions that stabilize the negatively charged groups. The enzyme exhibits a catalytic efficiency of 1.2 × 105 M -1s-1for the dehydration of 2-phospho-d-glycerate, which is comparable to the kinetic parameters of related enzymes. These results expand the understanding of the biophysical features of these enzymes, broadening the toolbox for metabolic engineering applications.
Fil: Gonzalez, Javier Marcelo. Universidad Nacional de Santiago del Estero. Instituto de Bionanotecnología del Noa. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto de Bionanotecnología del Noa; Argentina
Fil: Martí Arbona, Ricardo. Los Alamos National High Magnetic Field Laboratory; Estados Unidos
Fil: Chen, Julian C. H.. Los Alamos National High Magnetic Field Laboratory; Estados Unidos
Fil: Unkefer, Clifford. Los Alamos National High Magnetic Field Laboratory; Estados Unidos
description A structure-function characterization of Synechococcus elongatus enolase (SeEN) is presented, representing the first structural report on a cyanobacterial enolase. X-ray crystal structures of SeEN in its apoenzyme form and in complex with phosphoenolpyruvate are reported at 2.05 and 2.30 Å resolution, respectively. SeEN displays the typical fold of enolases, with a conformationally flexible loop that closes the active site upon substrate binding, assisted by two metal ions that stabilize the negatively charged groups. The enzyme exhibits a catalytic efficiency of 1.2 × 105 M -1s-1for the dehydration of 2-phospho-d-glycerate, which is comparable to the kinetic parameters of related enzymes. These results expand the understanding of the biophysical features of these enzymes, broadening the toolbox for metabolic engineering applications.
publishDate 2022
dc.date.none.fl_str_mv 2022-04
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/11336/213746
Gonzalez, Javier Marcelo; Martí Arbona, Ricardo; Chen, Julian C. H.; Unkefer, Clifford; The structure of Synechococcus elongatus enolase reveals key aspects of phosphoenolpyruvate binding; Wiley Blackwell Publishing, Inc; Acta Crystallographica Section F: Structural Biology Communications; 78; 4-2022; 177-184
2053-230X
CONICET Digital
CONICET
url http://hdl.handle.net/11336/213746
identifier_str_mv Gonzalez, Javier Marcelo; Martí Arbona, Ricardo; Chen, Julian C. H.; Unkefer, Clifford; The structure of Synechococcus elongatus enolase reveals key aspects of phosphoenolpyruvate binding; Wiley Blackwell Publishing, Inc; Acta Crystallographica Section F: Structural Biology Communications; 78; 4-2022; 177-184
2053-230X
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://scripts.iucr.org/cgi-bin/paper?S2053230X22003612
info:eu-repo/semantics/altIdentifier/doi/10.1107/S2053230X22003612
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 Wiley Blackwell Publishing, Inc
publisher.none.fl_str_mv Wiley Blackwell Publishing, 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
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score 13.070432

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