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dc.contributor.author
Wu, Rui
dc.contributor.author
Asención Diez, Matías Damián
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Figueroa, Carlos Miguel
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Machtey, Matías
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Iglesias, Alberto Alvaro
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Ballicora, Miguel A.
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Liu, Dali
dc.date.available
2018-03-27T21:07:17Z
dc.date.issued
2015-09
dc.identifier.citation
Wu, Rui; Asención Diez, Matías Damián; Figueroa, Carlos Miguel; Machtey, Matías; Iglesias, Alberto Alvaro; et al.; The crystal structure of Nitrosomonas europaea sucrose synthase reveals critical conformational changes and insights into sucrose metabolism in prokaryotes; American Society for Microbiology; Journal Of Bacteriology; 197; 17; 9-2015; 2734-2746
dc.identifier.issn
0021-9193
dc.identifier.uri
http://hdl.handle.net/11336/40268
dc.description.abstract
In this paper we report the first crystal structure of a prokaryotic sucrose synthase from the nonphotosynthetic bacterium Nitrosomonas europaea. The obtained structure was in an open form, whereas the only other available structure, from the plant Arabidopsis thaliana, was in a closed conformation. Comparative structural analysis revealed a "hinge-latch" combination, which is critical to transition between the open and closed forms of the enzyme. The N. europaea sucrose synthase shares the same fold as the GT-B family of the retaining glycosyltransferases. In addition, a triad of conserved homologous catalytic residues in the family was shown to be functionally critical in the N. europaea sucrose synthase (Arg567, Lys572, and Glu663). This implies that sucrose synthase shares not only a common origin with the GT-B family but also a similar catalytic mechanism. The enzyme preferred transferring glucose from ADP-glucose rather than UDP-glucose like the eukaryotic counterparts. This predicts that these prokaryotic organisms have a different sucrose metabolic scenario from plants. Nucleotide preference determines where the glucose moiety is targeted after sucrose is degraded.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
American Society for Microbiology
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Sucrose Metabolism
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Nitrosomonas
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Protein Structure
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Non-Photosynthetic Autotroph
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Otras Ciencias Biológicas
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
The crystal structure of Nitrosomonas europaea sucrose synthase reveals critical conformational changes and insights into sucrose metabolism in prokaryotes
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-03-21T16:53:18Z
dc.journal.volume
197
dc.journal.number
17
dc.journal.pagination
2734-2746
dc.journal.pais
Estados Unidos
dc.journal.ciudad
Washington
dc.description.fil
Fil: Wu, Rui. University of Chicago; Estados Unidos
dc.description.fil
Fil: Asención Diez, Matías Damián. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina. University of Chicago; Estados Unidos
dc.description.fil
Fil: Figueroa, Carlos Miguel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina. University of Chicago; Estados Unidos
dc.description.fil
Fil: Machtey, Matías. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina
dc.description.fil
Fil: Iglesias, Alberto Alvaro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Agrobiotecnología del Litoral. Universidad Nacional del Litoral. Instituto de Agrobiotecnología del Litoral; Argentina
dc.description.fil
Fil: Ballicora, Miguel A.. University of Chicago; Estados Unidos
dc.description.fil
Fil: Liu, Dali. University of Chicago; Estados Unidos
dc.journal.title
Journal Of Bacteriology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1128/JB.00110-15
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