Possible Metsulfuron Herbicide Detoxification by a Oryza sativa L. Glutathione S-transferase Enzyme.
Autor(a) principal: | |
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Data de Publicação: | 2020 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Brazilian Archives of Biology and Technology |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132020000100202 |
Resumo: | Abstract Rice (Oryza sativa L.) is one of the most important crops in the world, and it is considered the primary source of nutritional layout in developing countries in Asia. The glutathione S-transferases (GSTs) superfamily confers to rice protection against biotic and abiotic stress, and herbicide resistance. However, the three-dimensional structure of a GST Tau class, is unsolved. The objectives of this work were to develop a reliable comparative model for the s-transferase glutathione class Tau 4 from rice, and simulate docking interactions, against herbicides bentazon and metsulfuron. Results showed that the predicted model is reliable and has structural quality. Ramachandran plot set 91.9% of the residues in the most favored regions. All complexes showed negative binding energies values; and metsulfuron docked to the glutathione tripeptide, and it represents a possible insilico evidence of glutathione conjugation with this herbicide. |
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Brazilian Archives of Biology and Technology |
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Possible Metsulfuron Herbicide Detoxification by a Oryza sativa L. Glutathione S-transferase Enzyme.Molecular ModelingOsGSTHerbicideDockingBioinformaticsComputational BiologyAbstract Rice (Oryza sativa L.) is one of the most important crops in the world, and it is considered the primary source of nutritional layout in developing countries in Asia. The glutathione S-transferases (GSTs) superfamily confers to rice protection against biotic and abiotic stress, and herbicide resistance. However, the three-dimensional structure of a GST Tau class, is unsolved. The objectives of this work were to develop a reliable comparative model for the s-transferase glutathione class Tau 4 from rice, and simulate docking interactions, against herbicides bentazon and metsulfuron. Results showed that the predicted model is reliable and has structural quality. Ramachandran plot set 91.9% of the residues in the most favored regions. All complexes showed negative binding energies values; and metsulfuron docked to the glutathione tripeptide, and it represents a possible insilico evidence of glutathione conjugation with this herbicide.Instituto de Tecnologia do Paraná - Tecpar2020-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132020000100202Brazilian Archives of Biology and Technology v.63 2020reponame:Brazilian Archives of Biology and Technologyinstname:Instituto de Tecnologia do Paraná (Tecpar)instacron:TECPAR10.1590/1678-4324-2020180571info:eu-repo/semantics/openAccessAmador,Vinícius CostaSilva,Edson Ferreira daNadvorny,DanielaMaia,Rafael Trindadeeng2020-05-04T00:00:00Zoai:scielo:S1516-89132020000100202Revistahttps://www.scielo.br/j/babt/https://old.scielo.br/oai/scielo-oai.phpbabt@tecpar.br||babt@tecpar.br1678-43241516-8913opendoar:2020-05-04T00:00Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)false |
dc.title.none.fl_str_mv |
Possible Metsulfuron Herbicide Detoxification by a Oryza sativa L. Glutathione S-transferase Enzyme. |
title |
Possible Metsulfuron Herbicide Detoxification by a Oryza sativa L. Glutathione S-transferase Enzyme. |
spellingShingle |
Possible Metsulfuron Herbicide Detoxification by a Oryza sativa L. Glutathione S-transferase Enzyme. Amador,Vinícius Costa Molecular Modeling OsGST Herbicide Docking Bioinformatics Computational Biology |
title_short |
Possible Metsulfuron Herbicide Detoxification by a Oryza sativa L. Glutathione S-transferase Enzyme. |
title_full |
Possible Metsulfuron Herbicide Detoxification by a Oryza sativa L. Glutathione S-transferase Enzyme. |
title_fullStr |
Possible Metsulfuron Herbicide Detoxification by a Oryza sativa L. Glutathione S-transferase Enzyme. |
title_full_unstemmed |
Possible Metsulfuron Herbicide Detoxification by a Oryza sativa L. Glutathione S-transferase Enzyme. |
title_sort |
Possible Metsulfuron Herbicide Detoxification by a Oryza sativa L. Glutathione S-transferase Enzyme. |
author |
Amador,Vinícius Costa |
author_facet |
Amador,Vinícius Costa Silva,Edson Ferreira da Nadvorny,Daniela Maia,Rafael Trindade |
author_role |
author |
author2 |
Silva,Edson Ferreira da Nadvorny,Daniela Maia,Rafael Trindade |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Amador,Vinícius Costa Silva,Edson Ferreira da Nadvorny,Daniela Maia,Rafael Trindade |
dc.subject.por.fl_str_mv |
Molecular Modeling OsGST Herbicide Docking Bioinformatics Computational Biology |
topic |
Molecular Modeling OsGST Herbicide Docking Bioinformatics Computational Biology |
description |
Abstract Rice (Oryza sativa L.) is one of the most important crops in the world, and it is considered the primary source of nutritional layout in developing countries in Asia. The glutathione S-transferases (GSTs) superfamily confers to rice protection against biotic and abiotic stress, and herbicide resistance. However, the three-dimensional structure of a GST Tau class, is unsolved. The objectives of this work were to develop a reliable comparative model for the s-transferase glutathione class Tau 4 from rice, and simulate docking interactions, against herbicides bentazon and metsulfuron. Results showed that the predicted model is reliable and has structural quality. Ramachandran plot set 91.9% of the residues in the most favored regions. All complexes showed negative binding energies values; and metsulfuron docked to the glutathione tripeptide, and it represents a possible insilico evidence of glutathione conjugation with this herbicide. |
publishDate |
2020 |
dc.date.none.fl_str_mv |
2020-01-01 |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132020000100202 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132020000100202 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/1678-4324-2020180571 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
text/html |
dc.publisher.none.fl_str_mv |
Instituto de Tecnologia do Paraná - Tecpar |
publisher.none.fl_str_mv |
Instituto de Tecnologia do Paraná - Tecpar |
dc.source.none.fl_str_mv |
Brazilian Archives of Biology and Technology v.63 2020 reponame:Brazilian Archives of Biology and Technology instname:Instituto de Tecnologia do Paraná (Tecpar) instacron:TECPAR |
instname_str |
Instituto de Tecnologia do Paraná (Tecpar) |
instacron_str |
TECPAR |
institution |
TECPAR |
reponame_str |
Brazilian Archives of Biology and Technology |
collection |
Brazilian Archives of Biology and Technology |
repository.name.fl_str_mv |
Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar) |
repository.mail.fl_str_mv |
babt@tecpar.br||babt@tecpar.br |
_version_ |
1750318279627374592 |