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Registro Completo |
Biblioteca(s): |
Embrapa Agricultura Digital. |
Data corrente: |
26/11/2009 |
Data da última atualização: |
15/01/2020 |
Tipo da produção científica: |
Resumo em Anais de Congresso |
Autoria: |
CAMINHA, I. P.; FALCÃO, P. K.; TEIXEIRA, K. R. |
Afiliação: |
ISABEL PEREIRA CAMINHA, Estagiária/CNPTIA; PAULA REGINA KUSER FALCAO, CNPTIA; KATIA REGINA DOS SANTOS TEIXEIRA, CNPAB. |
Título: |
Structural studies of Gluconate 5-dehydrogenase from gluconacetobacter diazotrophicus. |
Ano de publicação: |
2009 |
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. |
Páginas: |
Não paginado. |
Idioma: |
Inglês |
Notas: |
X-Meeting 2009. |
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 |
Palavras-Chave: |
Bioinformática; BLAST; GROMACS; Modelagem. |
Thesagro: |
Genoma; Proteína; Simulação. |
Thesaurus Nal: |
Bioinformatics; Models. |
Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
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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Embrapa Agricultura Digital (CNPTIA) |
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Biblioteca(s): |
Embrapa Milho e Sorgo; Embrapa Unidades Centrais. |
Data corrente: |
30/10/2000 |
Data da última atualização: |
11/12/2021 |
Autoria: |
CARVALHO, H. W. L. de; LEAL, M. de L. da S.; GUIMARAES, P. E. de O.; SANTOS, M. X. dos; CARVALHO, P. C. L. de. |
Afiliação: |
HELIO WILSON LEMOS DE CARVALHO, CPATC; PAULO EVARISTO DE O GUIMARAES, CNPMS. |
Título: |
Três ciclos de seleção entre e dentro de progênies de meios-irmãos na população de milho CMS-52. |
Ano de publicação: |
2000 |
Fonte/Imprenta: |
Pesquisa Agropecuária Brasileira, Brasília, v. 35, n. 8, p. 1621-1628, 2000. |
Idioma: |
Português |
Conteúdo: |
Tres ciclos de selecao entre e dentro de progenies de meios-irmaos foram praticados na populacao de milho (Zea mays L.) de alta qualidade proteica CMS-52, nos tabuleiros costeiros dos estados de Sergipe e Bahia, no periodo de 1995 a 1997, visando a obtencao de uma populacao melhor adaptadas as condicoes edafoclimaticas da regiao. As progenies foram avaliadas em latice simples 14 x 14, com recombinacao das progenies superiores, dentro do mesmo ano agricola, de modo a se obter um ciclo por ano. Os valores dos parametros geneticos decresceram do ciclo original para o ciclo I, mantendo-se no ciclo II com magnitudes semelhantes ao ciclo I. As altas magnitudes desses parametros geneticos, as altas medias de produtividade das progenies, e o ganho medio esperado com a selecao entre e dentro de progenies, por ciclo de selecao (12,3%), mostram o grande potencial da populacao em responder a selecao, o que permitira a obtencao de uma populacao mais produtiva e melhor adaptada as condicoes edafoclimaticas da regiao. A magnitude da interacao progenies x locais evidenciou a importancia de se avaliarem as progenies em mais de um local, para melhorar a eficiencia do processo seletivo e obter estimativas mais consistentes dos componentes da variancia. |
Palavras-Chave: |
Genetic parameters; Maize; Parametros geneticos; Selection. |
Thesagro: |
Genética; Melhoramento; Método de Melhoramento; Milho; Parâmetro Genético; Seleção; Teste de Progênie; Variação Genética; Zea Mays. |
Thesaurus NAL: |
breeding; Breeding methods; Corn; Genetic variation; Genetics; Progeny testing. |
Categoria do assunto: |
-- G Melhoramento Genético |
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/AI-SEDE/18397/1/pab98_323.pdf
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Marc: |
LEADER 02381naa a2200397 a 4500 001 1484397 005 2021-12-11 008 2000 bl uuuu u00u1 u #d 100 1 $aCARVALHO, H. W. L. de 245 $aTrês ciclos de seleção entre e dentro de progênies de meios-irmãos na população de milho CMS-52. 260 $c2000 520 $aTres ciclos de selecao entre e dentro de progenies de meios-irmaos foram praticados na populacao de milho (Zea mays L.) de alta qualidade proteica CMS-52, nos tabuleiros costeiros dos estados de Sergipe e Bahia, no periodo de 1995 a 1997, visando a obtencao de uma populacao melhor adaptadas as condicoes edafoclimaticas da regiao. As progenies foram avaliadas em latice simples 14 x 14, com recombinacao das progenies superiores, dentro do mesmo ano agricola, de modo a se obter um ciclo por ano. Os valores dos parametros geneticos decresceram do ciclo original para o ciclo I, mantendo-se no ciclo II com magnitudes semelhantes ao ciclo I. As altas magnitudes desses parametros geneticos, as altas medias de produtividade das progenies, e o ganho medio esperado com a selecao entre e dentro de progenies, por ciclo de selecao (12,3%), mostram o grande potencial da populacao em responder a selecao, o que permitira a obtencao de uma populacao mais produtiva e melhor adaptada as condicoes edafoclimaticas da regiao. A magnitude da interacao progenies x locais evidenciou a importancia de se avaliarem as progenies em mais de um local, para melhorar a eficiencia do processo seletivo e obter estimativas mais consistentes dos componentes da variancia. 650 $abreeding 650 $aBreeding methods 650 $aCorn 650 $aGenetic variation 650 $aGenetics 650 $aProgeny testing 650 $aGenética 650 $aMelhoramento 650 $aMétodo de Melhoramento 650 $aMilho 650 $aParâmetro Genético 650 $aSeleção 650 $aTeste de Progênie 650 $aVariação Genética 650 $aZea Mays 653 $aGenetic parameters 653 $aMaize 653 $aParametros geneticos 653 $aSelection 700 1 $aLEAL, M. de L. da S. 700 1 $aGUIMARAES, P. E. de O. 700 1 $aSANTOS, M. X. dos 700 1 $aCARVALHO, P. C. L. de 773 $tPesquisa Agropecuária Brasileira, Brasília$gv. 35, n. 8, p. 1621-1628, 2000.
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Embrapa Milho e Sorgo (CNPMS) |
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