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dc.contributor.author
Hill, B. L.
dc.contributor.author
Mascarenhas, R.
dc.contributor.author
Patel, H. P.
dc.contributor.author
Asención Diez, Matías Damián
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dc.contributor.author
Wu, R.
dc.contributor.author
Iglesias, Alberto Alvaro
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dc.contributor.author
Liu, D.
dc.contributor.author
Ballicora, M. A.
dc.date.available
2020-11-23T20:42:05Z
dc.date.issued
2019-01
dc.identifier.citation
Hill, B. L.; Mascarenhas, R.; Patel, H. P.; Asención Diez, Matías Damián; Wu, R.; et al.; Structural analysis reveals a pyruvate-binding activator site in the Agrobacterium tumefaciens ADP–glucose pyrophosphorylase; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 294; 1-2019; 1338-1348
dc.identifier.issn
0021-9258
dc.identifier.uri
http://hdl.handle.net/11336/118795
dc.description.abstract
The pathways for biosynthesis of glycogen inbacteria and starch in plants are evolutionarily andbiochemically related. They are regulated primarily by ADP?glucose pyrophosphorylase, which evolved to satisfy metabolic requirements of a particular organism. Despite the importance of these two pathways, little is known about the mechanism that controls pyrophosphorylase activity or the location of its allosteric sites. Here, we report pyruvate-bound crystal structures of ADP-glucose pyrophosphorylase from the bacterium Agrobacterium tumefaciens, identifying a previously elusive activator site for the enzyme. We found that the tetrameric enzyme binds two molecules of pyruvate in a planar conformation. Each binding site is located in a crevice between the C-terminal domains of two subunits where they stack via a distinct β-helix region. Pyruvate interacts with the side chain of Lys-43 and with the peptide backbone of Ser-328 and Gly-329 from both subunits. These structural insights led to the design of two variants with altered regulator properties. In one variant (K43A), the allosteric effect was absent, whereas in the other (G329D), the introduced Asp mimicked the presence of pyruvate. The latter generated an enzyme that was pre-activated and insensitive to further activation by pyruvate. Our study furnishes a deeper understanding of how glycogen biosynthesis is regulated in bacteria and the mechanism by which transgenic plants increased their starch production. These insights will facilitate rational approaches to enzyme engineering for starch production in crops of agricultural interest and will promote further study of allosteric signal transmission and molecular evolution in this important enzyme family.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
American Society for Biochemistry and Molecular Biology
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE
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GLYCOGEN BIOSYNTHESIS
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STARCH BIOSYNTHESIS
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ALLOSTERISM
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ENZYME EVOLUTION
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GLUCAN BIOSYNTHESIS
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
Structural analysis reveals a pyruvate-binding activator site in the Agrobacterium tumefaciens ADP–glucose pyrophosphorylase
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2020-11-20T20:00:32Z
dc.journal.volume
294
dc.journal.pagination
1338-1348
dc.journal.pais
Estados Unidos
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dc.journal.ciudad
Bethesda, Maryland
dc.description.fil
Fil: Hill, B. L.. Dpt Of Chem And Biochemistry. Loyola University Chicago; Estados Unidos
dc.description.fil
Fil: Mascarenhas, R.. Dpt Of Chem And Biochemistry. Loyola University Chicago; Estados Unidos
dc.description.fil
Fil: Patel, H. P.. Dpt Of Chem And Biochemistry. Loyola University Chicago; Estados Unidos
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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
dc.description.fil
Fil: Wu, R.. Dpt Of Chem And Biochemistry. Loyola University Chicago; Estados Unidos
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: Liu, D.. Dpt Of Chem And Biochemistry. Loyola University Chicago; Estados Unidos
dc.description.fil
Fil: Ballicora, M. A.. Dpt Of Chem And Biochemistry. Loyola University Chicago; Estados Unidos
dc.journal.title
Journal of Biological Chemistry (online)
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/lookup/doi/10.1074/jbc.RA118.004246
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1074/jbc.RA118.004246
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