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 | Acesso ao texto completo restrito à biblioteca da Embrapa Agricultura Digital. Para informações adicionais entre em contato com cnptia.biblioteca@embrapa.br. |
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Registro Completo |
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Biblioteca(s): |
Embrapa Agricultura Digital. |
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Data corrente: |
26/11/2009 |
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Data da última atualização: |
15/01/2020 |
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Tipo da produção científica: |
Resumo em Anais de Congresso |
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Autoria: |
CAMINHA, I. P.; FALCÃO, P. K.; TEIXEIRA, K. R. |
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Afiliação: |
ISABEL PEREIRA CAMINHA, Estagiária/CNPTIA; PAULA REGINA KUSER FALCAO, CNPTIA; KATIA REGINA DOS SANTOS TEIXEIRA, CNPAB. |
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Título: |
Structural studies of Gluconate 5-dehydrogenase from gluconacetobacter diazotrophicus. |
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Ano de publicação: |
2009 |
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Fonte/Imprenta: |
In: INTERNATIONAL CONFERENCE OF THE BRAZILIAN ASSOCIATION FOR BIOINFORMATICS AND COMPUTATIONAL BIOLOGY, 5., 2009, Angra dos Reis. Abstracts book... Angra dos Reis: ABBCB, 2009. |
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Páginas: |
Não paginado. |
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Idioma: |
Inglês |
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Notas: |
X-Meeting 2009. |
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Conteúdo: |
The recent sequencing of the Gluconacetobacter diazotrophicus genome, developed by Projeto RioGene, permits a search by ORFs related to organic acid production. In this study, a putative Gluconate 5-dehydrogenase (Ga5DH) ORF, A9H995, was selected. Ga5DH is an enzyme that plays an important role in regulating the flux of carbon and energy source in bacteria, and in the production of organic acids, among them the 5-keto-D-Gluconate (5KGA). Due to the fundamental role of this acid in the chemical industry, like the precursor to tartaric acid production for example, there is a large interest in respect to the structure of this protein since there is little physical or structural information available about it. To this end, we herein report the theoretical structure of Ga5DH from Gluconacetobacter diazotrophicus. This structure was obtained through in silico studies if the three-dimensional structure generated by homology modelling. The sequence alignment program BLAST was used to search homologous sequences against the Protein Data Bank (PDB), and the best template was chosen according to the sequence identity (ID). The reference structure used was the crystal structure of Ga5DH from Streptococcus suis species (PDB 3cxr:A). This protein wich belongs to the family of short-chain dehydrogenases/reductases (SDR), presented 42% identity with Ga5DH from G. diazotrophicus. By using the programa MODELLER9v6, ten models were built and the best model was determined by the lowest value of objective function. LIGPLOT was used to identify the interactions with possible ligants of this enzyme. A comparative analysis shows that the residues from S. Suis which are involved in ligand binding (GKR D-glucarate and NAP NADP Nicotinamide-adenine-dinucleotide-phosphate) are conserved both sequentially and structurally. This may suggests that the target sequence has the same ligands. Molecular dynamics simulations were performed with GROMACS software package. The residues involved in the interaction with the substrate were replaced by alanine, and the model with mutated amino acids was further submitted to molecular dynamics simulations to gain insights into affinities, contacts and stability of the essencial amino acids for structure and function of this enzyme, as well as information on the binding profile. MenosThe recent sequencing of the Gluconacetobacter diazotrophicus genome, developed by Projeto RioGene, permits a search by ORFs related to organic acid production. In this study, a putative Gluconate 5-dehydrogenase (Ga5DH) ORF, A9H995, was selected. Ga5DH is an enzyme that plays an important role in regulating the flux of carbon and energy source in bacteria, and in the production of organic acids, among them the 5-keto-D-Gluconate (5KGA). Due to the fundamental role of this acid in the chemical industry, like the precursor to tartaric acid production for example, there is a large interest in respect to the structure of this protein since there is little physical or structural information available about it. To this end, we herein report the theoretical structure of Ga5DH from Gluconacetobacter diazotrophicus. This structure was obtained through in silico studies if the three-dimensional structure generated by homology modelling. The sequence alignment program BLAST was used to search homologous sequences against the Protein Data Bank (PDB), and the best template was chosen according to the sequence identity (ID). The reference structure used was the crystal structure of Ga5DH from Streptococcus suis species (PDB 3cxr:A). This protein wich belongs to the family of short-chain dehydrogenases/reductases (SDR), presented 42% identity with Ga5DH from G. diazotrophicus. By using the programa MODELLER9v6, ten models were built and the best model was determined by the lowest value of... Mostrar Tudo |
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Palavras-Chave: |
Bioinformática; BLAST; GROMACS; Modelagem. |
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Thesagro: |
Genoma; Proteína; Simulação. |
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Thesaurus Nal: |
Bioinformatics; Models. |
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Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
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Marc: |
LEADER 03173nam a2200265 a 4500
001 1576243
005 2020-01-15
008 2009 bl uuuu u00u1 u #d
100 1 $aCAMINHA, I. P.
245 $aStructural studies of Gluconate 5-dehydrogenase from gluconacetobacter diazotrophicus.$h[electronic resource]
260 $aIn: INTERNATIONAL CONFERENCE OF THE BRAZILIAN ASSOCIATION FOR BIOINFORMATICS AND COMPUTATIONAL BIOLOGY, 5., 2009, Angra dos Reis. Abstracts book... Angra dos Reis: ABBCB$c2009
300 $aNão paginado.
500 $aX-Meeting 2009.
520 $aThe recent sequencing of the Gluconacetobacter diazotrophicus genome, developed by Projeto RioGene, permits a search by ORFs related to organic acid production. In this study, a putative Gluconate 5-dehydrogenase (Ga5DH) ORF, A9H995, was selected. Ga5DH is an enzyme that plays an important role in regulating the flux of carbon and energy source in bacteria, and in the production of organic acids, among them the 5-keto-D-Gluconate (5KGA). Due to the fundamental role of this acid in the chemical industry, like the precursor to tartaric acid production for example, there is a large interest in respect to the structure of this protein since there is little physical or structural information available about it. To this end, we herein report the theoretical structure of Ga5DH from Gluconacetobacter diazotrophicus. This structure was obtained through in silico studies if the three-dimensional structure generated by homology modelling. The sequence alignment program BLAST was used to search homologous sequences against the Protein Data Bank (PDB), and the best template was chosen according to the sequence identity (ID). The reference structure used was the crystal structure of Ga5DH from Streptococcus suis species (PDB 3cxr:A). This protein wich belongs to the family of short-chain dehydrogenases/reductases (SDR), presented 42% identity with Ga5DH from G. diazotrophicus. By using the programa MODELLER9v6, ten models were built and the best model was determined by the lowest value of objective function. LIGPLOT was used to identify the interactions with possible ligants of this enzyme. A comparative analysis shows that the residues from S. Suis which are involved in ligand binding (GKR D-glucarate and NAP NADP Nicotinamide-adenine-dinucleotide-phosphate) are conserved both sequentially and structurally. This may suggests that the target sequence has the same ligands. Molecular dynamics simulations were performed with GROMACS software package. The residues involved in the interaction with the substrate were replaced by alanine, and the model with mutated amino acids was further submitted to molecular dynamics simulations to gain insights into affinities, contacts and stability of the essencial amino acids for structure and function of this enzyme, as well as information on the binding profile.
650 $aBioinformatics
650 $aModels
650 $aGenoma
650 $aProteína
650 $aSimulação
653 $aBioinformática
653 $aBLAST
653 $aGROMACS
653 $aModelagem
700 1 $aFALCÃO, P. K.
700 1 $aTEIXEIRA, K. R.
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Registro original: |
Embrapa Agricultura Digital (CNPTIA) |
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| Registros recuperados : 12 | |
| 3. |  | SAVINI, T. C.; CONCEIÇÃO, M. A. F.; SANTOS, C. P. dos; SOUZA, R. T. de. Efeito da suspensão da irrigação sobre a incidência de requeima na cultivar de videira Niágara Rosada. In: ENCONTRO DE INICIAÇÃO CIENTÍFICA DA EMBRAPA UVA E VINHO, 12., ENCONTRO DE PÓS-GRADUANDOS DA EMBRAPA UVA E VINHO, 8., 2014, Bento Gonçalves. Resumos... Bento Gonçalves: Embrapa Uva e Vinho, 2014. p. 56| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Uva e Vinho. |
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| 4. | | SANTOS, C. P. dos; SOUZA, R. T. de; SAVINI, T. C.; CONCEIÇÃO, M. A. F. Formação do vinhedo com a cultivar BRS Isis no sistema de sustentação em Y, sobre diferentes porta-enxertos. In: ENCONTRO DE INICIAÇÃO CIENTÍFICA DA EMBRAPA UVA E VINHO, 12., ENCONTRO DE PÓS-GRADUANDOS DA EMBRAPA UVA E VINHO, 8., 2014, Bento Gonçalves. Resumos... Bento Gonçalves: Embrapa Uva e Vinho, 2014. p. 58| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Uva e Vinho. |
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| 6. | | SOUZA, R. T. de; SANTOS, C. P. DOS; SAVINI, T. C.; COSTA, S. M. DA; CONCEIÇÃO, M. A. F. Formação do vinhedo com a cultivar BRS Vtória no sistema de condução em y, sobre diferentes porta-enxertos. CONGRESSO BRASILEIRO DE FRUTICULTURA, 23., 2014, Cuiabá. Fruticultura: oportunidades e desafios para o Brasil: anais. Cuiabá: SBF: UFMT: CREA-MT: MAPA, 2014.TRA3680. 4 p.| Tipo: Artigo em Anais de Congresso |
| Biblioteca(s): Embrapa Uva e Vinho. |
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| 7. | | PEREIRA, D.; MANSUR, M. C. D.; VOLKMER-RIBEIRO, C.; OLIVEIRA, M. D. de; SANTOS, C. P. dos; BERGONCI, P. E. A. Colonização de substrato artificial por macroinvertebrados límnicos, no delta do rio Jacuí (RS, Brasil). Revista Biotemas, v. 23, n.1, mar., 2010.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: B - 3 |
| Biblioteca(s): Embrapa Pantanal. |
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| 8. | | ANJOS, A. M. R. dos; MARTINS JUNIOR, H.; SANTOS, C. P. dos; CORREA, R. de O.; COSTA, S. M. da; SOUZA, C. F. de; LIMA, G. R. L. Desempenho em ganho de peso de tambaquis (Colossoma macropomum) arraçoados com ração à base de farelo de coco. In: CONGRESSO DA SOCIEDADE BRASILEIRA DE AQUICULTURA E BIOLOGIA AQUÁTICA, 7., 2010, Recife. Anais... Jaboticabal: Sociedade Brasileira de Aquicultura, 2010.| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Amazônia Oriental. |
|  |
| 9. | | SANTOS, C. P. dos; GOMES, T. R. C.; COSTA, L. R. S.; PEREIRA NETO, L. G.; JOSÉ, S. C. B. R. Determinação da curva de secagem de sementes de pinhão manso (Jatropha curcas L). In: SIMPÓSIO BRASILEIRO DE RECURSOS GENÉTICOS, 2., 2008, Brasília, DF. Anais... Brasília, DF: Embrapa Recursos Genéticos e Biotecnologia: Fundação de Apoio à Pesquisa Científica e Tecnológica - FUNCREDI, 2008. p.326.| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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| 10. | | SANTOS, C. P. dos; OLIVEIRA, T. C. de; PINTO, J. A. O.; FONTES, S. S.; CRUZ, E. M. O.; ARRIGONI BLANK, M. de F.; ANDRADE, T. M.; MATOS, I. L. de; ALVES, P. B.; INNECCO, R.; BLANK, A. F. Chemical diversity and influence of plant age on the essential oil from Lippia sidoides Cham. germplasm. Industrial Crops and Products, v. 76, p. 416-421, 2015.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 1 |
| Biblioteca(s): Embrapa Tabuleiros Costeiros. |
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| 12. | | MARTINS JUNIOR, H.; CORREA, R. de O.; MEYER, G.; LIMA, G. R.; ANJOS, A. M. R. dos; SOUZA, C. F. de; COSTA, S. M. da; SANTOS, C. P. dos. O uso da macaxeira e do farelo de soja como alternativa ao arraçoamento do tambaqui (Colossoma Macropomum, Cuvier 1818). In: CONGRESSO DA SOCIEDADE BRASILEIRA DE AQUICULTURA E BIOLOGIA AQUÁTICA, 7., 2010, Recife. Anais... Jaboticabal: Sociedade Brasileira de Aquicultura, 2010.| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Amazônia Oriental. |
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| Registros recuperados : 12 | |
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| Nenhum registro encontrado para a expressão de busca informada. |
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