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dc.contributor.author
Gonzalez, Javier Marcelo
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dc.contributor.author
Martí Arbona, Ricardo
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dc.contributor.author
Chen, Julian
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dc.contributor.author
Broom Peltz, Brian
dc.contributor.author
Unkefer, Clifford
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dc.date.available
2019-12-18T13:07:09Z
dc.date.issued
2018-10
dc.identifier.citation
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
dc.identifier.issn
2053-230X
dc.identifier.uri
http://hdl.handle.net/11336/92464
dc.description.abstract
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.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
International Union of Crystallography
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
BIOFUELS
dc.subject
MALATE DEHYDROGENASE
dc.subject
METHYLOBACTERIUM EXTORQUENS
dc.subject
METHYLOTROPHS
dc.subject.classification
Bioquímica y Biología Molecular
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Conformational changes on substrate binding revealed by structures of Methylobacterium extorquens malate dehydrogenase
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-10-22T15:53:18Z
dc.journal.volume
74
dc.journal.number
10
dc.journal.pagination
610-616
dc.journal.pais
Reino Unido
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dc.journal.ciudad
Londres
dc.description.fil
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
dc.description.fil
Fil: Marti Arbona, R.. Bioscience Division, Los Alamos National Laboratory; Estados Unidos
dc.description.fil
Fil: Chen, J. C. H.. Bioscience Division, Los Alamos National Laboratory; Estados Unidos
dc.description.fil
Fil: Broom Peltz, B.. Bioscience Division, Los Alamos National Laboratory; Estados Unidos
dc.description.fil
Fil: Unkefer, C. J.. Bioscience Division, Los Alamos National Laboratory; Estados Unidos
dc.journal.title
Acta Crystallographica Section F: Structural Biology Communications
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1107/S2053230X18011809
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://scripts.iucr.org/cgi-bin/paper?S2053230X18011809
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6168771/
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