Conformational changes on substrate binding revealed by structures of Methylobacterium extorquens malate dehydrogenase
- Autores
- Gonzalez, Javier Marcelo; Martí Arbona, Ricardo; Chen, Julian; Broom Peltz, Brian; Unkefer, Clifford
- Año de publicación
- 2018
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Three high-resolution X-ray crystal structures of malate dehydrogenase (MDH; EC 1.1.1.37) from the methylotroph Methylobacterium extorquens AM1 are presented. By comparing the structures of apo MDH, a binary complex of MDH and NAD+, and a ternary complex of MDH and oxaloacetate with ADP-ribose occupying the pyridine nucleotide-binding site, conformational changes associated with the formation of the catalytic complex were characterized. While the substrate-binding site is accessible in the enzyme resting state or NAD+-bound forms, the substrate-bound form exhibits a closed conformation. This conformational change involves the transition of an α-helix to a 310-helix, which causes the adjacent loop to close the active site following coenzyme and substrate binding. In the ternary complex, His284 forms a hydrogen bond to the C2 carbonyl of oxaloacetate, placing it in a position to donate a proton in the formation of (2S)-malate.Crystal structures of apo malate dehydrogenase (MDH) from Methylobacterium extorquens, MDH bound to NAD+, and MDH with oxaloacetate and ADP-ribose revealed conformational changes, closing the active site upon coenzyme and substrate binding. In the ternary complex, His284 is in position to donate a proton in the formation of (2S)-malate.
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: Marti Arbona, R.. Bioscience Division, Los Alamos National Laboratory; Estados Unidos
Fil: Chen, J. C. H.. Bioscience Division, Los Alamos National Laboratory; Estados Unidos
Fil: Broom Peltz, B.. Bioscience Division, Los Alamos National Laboratory; Estados Unidos
Fil: Unkefer, C. J.. Bioscience Division, Los Alamos National Laboratory; Estados Unidos - Materia
-
BIOFUELS
MALATE DEHYDROGENASE
METHYLOBACTERIUM EXTORQUENS
METHYLOTROPHS - 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:11336/92464
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Conformational changes on substrate binding revealed by structures of Methylobacterium extorquens malate dehydrogenaseGonzalez, Javier MarceloMartí Arbona, RicardoChen, JulianBroom Peltz, BrianUnkefer, CliffordBIOFUELSMALATE DEHYDROGENASEMETHYLOBACTERIUM EXTORQUENSMETHYLOTROPHShttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Three high-resolution X-ray crystal structures of malate dehydrogenase (MDH; EC 1.1.1.37) from the methylotroph Methylobacterium extorquens AM1 are presented. By comparing the structures of apo MDH, a binary complex of MDH and NAD+, and a ternary complex of MDH and oxaloacetate with ADP-ribose occupying the pyridine nucleotide-binding site, conformational changes associated with the formation of the catalytic complex were characterized. While the substrate-binding site is accessible in the enzyme resting state or NAD+-bound forms, the substrate-bound form exhibits a closed conformation. This conformational change involves the transition of an α-helix to a 310-helix, which causes the adjacent loop to close the active site following coenzyme and substrate binding. In the ternary complex, His284 forms a hydrogen bond to the C2 carbonyl of oxaloacetate, placing it in a position to donate a proton in the formation of (2S)-malate.Crystal structures of apo malate dehydrogenase (MDH) from Methylobacterium extorquens, MDH bound to NAD+, and MDH with oxaloacetate and ADP-ribose revealed conformational changes, closing the active site upon coenzyme and substrate binding. In the ternary complex, His284 is in position to donate a proton in the formation of (2S)-malate.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: Marti Arbona, R.. Bioscience Division, Los Alamos National Laboratory; Estados UnidosFil: Chen, J. C. H.. Bioscience Division, Los Alamos National Laboratory; Estados UnidosFil: Broom Peltz, B.. Bioscience Division, Los Alamos National Laboratory; Estados UnidosFil: Unkefer, C. J.. Bioscience Division, Los Alamos National Laboratory; Estados UnidosInternational Union of Crystallography2018-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/92464Gonzalez, Javier Marcelo; Martí Arbona, Ricardo; Chen, Julian; Broom Peltz, Brian; Unkefer, Clifford; Conformational changes on substrate binding revealed by structures of Methylobacterium extorquens malate dehydrogenase; International Union of Crystallography; Acta Crystallographica Section F: Structural Biology Communications; 74; 10; 10-2018; 610-6162053-230XCONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1107/S2053230X18011809info:eu-repo/semantics/altIdentifier/url/http://scripts.iucr.org/cgi-bin/paper?S2053230X18011809info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6168771/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:00:50Zoai:ri.conicet.gov.ar:11336/92464instacron: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 10:00:50.577CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Conformational changes on substrate binding revealed by structures of Methylobacterium extorquens malate dehydrogenase |
title |
Conformational changes on substrate binding revealed by structures of Methylobacterium extorquens malate dehydrogenase |
spellingShingle |
Conformational changes on substrate binding revealed by structures of Methylobacterium extorquens malate dehydrogenase Gonzalez, Javier Marcelo BIOFUELS MALATE DEHYDROGENASE METHYLOBACTERIUM EXTORQUENS METHYLOTROPHS |
title_short |
Conformational changes on substrate binding revealed by structures of Methylobacterium extorquens malate dehydrogenase |
title_full |
Conformational changes on substrate binding revealed by structures of Methylobacterium extorquens malate dehydrogenase |
title_fullStr |
Conformational changes on substrate binding revealed by structures of Methylobacterium extorquens malate dehydrogenase |
title_full_unstemmed |
Conformational changes on substrate binding revealed by structures of Methylobacterium extorquens malate dehydrogenase |
title_sort |
Conformational changes on substrate binding revealed by structures of Methylobacterium extorquens malate dehydrogenase |
dc.creator.none.fl_str_mv |
Gonzalez, Javier Marcelo Martí Arbona, Ricardo Chen, Julian Broom Peltz, Brian Unkefer, Clifford |
author |
Gonzalez, Javier Marcelo |
author_facet |
Gonzalez, Javier Marcelo Martí Arbona, Ricardo Chen, Julian Broom Peltz, Brian Unkefer, Clifford |
author_role |
author |
author2 |
Martí Arbona, Ricardo Chen, Julian Broom Peltz, Brian Unkefer, Clifford |
author2_role |
author author author author |
dc.subject.none.fl_str_mv |
BIOFUELS MALATE DEHYDROGENASE METHYLOBACTERIUM EXTORQUENS METHYLOTROPHS |
topic |
BIOFUELS MALATE DEHYDROGENASE METHYLOBACTERIUM EXTORQUENS METHYLOTROPHS |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Three high-resolution X-ray crystal structures of malate dehydrogenase (MDH; EC 1.1.1.37) from the methylotroph Methylobacterium extorquens AM1 are presented. By comparing the structures of apo MDH, a binary complex of MDH and NAD+, and a ternary complex of MDH and oxaloacetate with ADP-ribose occupying the pyridine nucleotide-binding site, conformational changes associated with the formation of the catalytic complex were characterized. While the substrate-binding site is accessible in the enzyme resting state or NAD+-bound forms, the substrate-bound form exhibits a closed conformation. This conformational change involves the transition of an α-helix to a 310-helix, which causes the adjacent loop to close the active site following coenzyme and substrate binding. In the ternary complex, His284 forms a hydrogen bond to the C2 carbonyl of oxaloacetate, placing it in a position to donate a proton in the formation of (2S)-malate.Crystal structures of apo malate dehydrogenase (MDH) from Methylobacterium extorquens, MDH bound to NAD+, and MDH with oxaloacetate and ADP-ribose revealed conformational changes, closing the active site upon coenzyme and substrate binding. In the ternary complex, His284 is in position to donate a proton in the formation of (2S)-malate. 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: Marti Arbona, R.. Bioscience Division, Los Alamos National Laboratory; Estados Unidos Fil: Chen, J. C. H.. Bioscience Division, Los Alamos National Laboratory; Estados Unidos Fil: Broom Peltz, B.. Bioscience Division, Los Alamos National Laboratory; Estados Unidos Fil: Unkefer, C. J.. Bioscience Division, Los Alamos National Laboratory; Estados Unidos |
description |
Three high-resolution X-ray crystal structures of malate dehydrogenase (MDH; EC 1.1.1.37) from the methylotroph Methylobacterium extorquens AM1 are presented. By comparing the structures of apo MDH, a binary complex of MDH and NAD+, and a ternary complex of MDH and oxaloacetate with ADP-ribose occupying the pyridine nucleotide-binding site, conformational changes associated with the formation of the catalytic complex were characterized. While the substrate-binding site is accessible in the enzyme resting state or NAD+-bound forms, the substrate-bound form exhibits a closed conformation. This conformational change involves the transition of an α-helix to a 310-helix, which causes the adjacent loop to close the active site following coenzyme and substrate binding. In the ternary complex, His284 forms a hydrogen bond to the C2 carbonyl of oxaloacetate, placing it in a position to donate a proton in the formation of (2S)-malate.Crystal structures of apo malate dehydrogenase (MDH) from Methylobacterium extorquens, MDH bound to NAD+, and MDH with oxaloacetate and ADP-ribose revealed conformational changes, closing the active site upon coenzyme and substrate binding. In the ternary complex, His284 is in position to donate a proton in the formation of (2S)-malate. |
publishDate |
2018 |
dc.date.none.fl_str_mv |
2018-10 |
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/11336/92464 Gonzalez, Javier Marcelo; Martí Arbona, Ricardo; Chen, Julian; Broom Peltz, Brian; Unkefer, Clifford; Conformational changes on substrate binding revealed by structures of Methylobacterium extorquens malate dehydrogenase; International Union of Crystallography; Acta Crystallographica Section F: Structural Biology Communications; 74; 10; 10-2018; 610-616 2053-230X CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/92464 |
identifier_str_mv |
Gonzalez, Javier Marcelo; Martí Arbona, Ricardo; Chen, Julian; Broom Peltz, Brian; Unkefer, Clifford; Conformational changes on substrate binding revealed by structures of Methylobacterium extorquens malate dehydrogenase; International Union of Crystallography; Acta Crystallographica Section F: Structural Biology Communications; 74; 10; 10-2018; 610-616 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/doi/10.1107/S2053230X18011809 info:eu-repo/semantics/altIdentifier/url/http://scripts.iucr.org/cgi-bin/paper?S2053230X18011809 info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6168771/ |
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 |
International Union of Crystallography |
publisher.none.fl_str_mv |
International Union of Crystallography |
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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1844613794516434944 |
score |
13.070432 |