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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: |
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Registro original: |
Embrapa Agricultura Digital (CNPTIA) |
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2. |  | SOUZA, P. E. de A.; BASTOS, A. P. A.; PRUDÊNCIO, C. R.; GASPAR, E. B.; CARVALHO, W. A. Análise da avidez de anticorpos contra SARS-CoV-2 em soro e colostro hiperimune. In: WORKSHOP DE INICIAÇÃO CIENTÍFICA DA EMBRAPA GADO DE LEITE - PIBIC/FAPEMIG, 30., 2024, Juiz de Fora. Anais [...]. Juiz de Fora: Embrapa Gado de Leite, 2025. p. 37-40. (Embrapa Gado de Leite. Eventos Técnicos & Científicos, 4). ODS 3.Tipo: Artigo em Anais de Congresso |
Biblioteca(s): Embrapa Gado de Leite. |
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3. |  | SOUZA, P. E. de A.; HONÓRIO, N. T. B. S.; DIAVÃO, J.; PRUDÊNCIO, C. R.; GASPAR, E. B.; BRANDAO, H. de M.; BASTOS, A. P. A.; CARVALHO, W. A. Colostro hiperimune: vacas como biofábricas de anticorpos neutralizantes contra SARS-CoV-2. In: ENCONTRO NACIONAL DA REDE DE PESQUISA E INOVAÇÃO EM SANIDADE E PECUÁRIA LEITEIRA, 2., 2024, Lavras. Mastite, qualidade do leite e queijo minas artesanal: anais do evento. Lavras: Universidade Federal de Lavras, 2024. p. 77.Tipo: Resumo em Anais de Congresso |
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4. |  | CARVALHO, W. A.; SOUZA, P. E. de A.; BASTOS, A. P. A.; SILVA, L. P. da; PRUDÊNCIO, C. R.; DIAVÃO, J.; CAMPOS, M. M.; BRANDAO, H. de M.; BONATTO, C. C.; GASPAR, E. B. Nanoparticle-based vaccine formulation and immunization strategy exploiting cows as biofactories for colostrum-derived neutralizing antibodies against SARSCoV2. In: INTERNATIONAL SYMPOSIUM ON IMMUNOBIOLOGICALS, 8., 2024, Rio de Janeiro. Abstracts [...]. Rio de Janeiro: Fundação Oswaldo Cruz, 2024. p. 72.Tipo: Resumo em Anais de Congresso |
Biblioteca(s): Embrapa Gado de Leite; Embrapa Recursos Genéticos e Biotecnologia; Embrapa Suínos e Aves. |
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5. |  | CARVALHO, W. A.; GASPAR, E. B.; PRUDENCIO, C. R.; SILVA, L. P. da; BONATTO, C.; BASTOS, A. P. A.; BRANDAO, H. de M.; DOMINGUES, R.; ORTS, D. J. B.; COSTA, H. H. M. da; GASPARI, E. de; FRANCO, A. L.; SILVA, A. S. Immunomodulatory nanosystems with active targeting to phagocytes promote the production of neutralizing antibodies against the SARCoV2 virus in cows' colostrum. In: CONGRESS OF THE BRAZILIAN SOCIETY OF IMMUNOLOGY, 47., 2023, Ouro Preto. Program. São Paulo: Sociedade Brasileira de Imunologia, 2023. p. 278. Immuno 2023.Tipo: Resumo em Anais de Congresso |
Biblioteca(s): Embrapa Gado de Leite; Embrapa Recursos Genéticos e Biotecnologia; Embrapa Suínos e Aves. |
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6. |  | SOUZA, P. E. de A.; MOREIRA, L. dos S.; CARVALHO, C. V. de; HONÓRIO, N. T. de B. S.; BASTOS, A. P. A.; SILVA, L. P. da; PRUDÊNCIO, C. R.; DOMINGUES, R.; GASPAR, E. B.; FRANCO, A. L.; REIS, D. R. de L.; BRANDAO, H. de M.; DIAVÃO, J.; SILVA, A. S.; CAMPOS, M. M.; CARVALHO, W. A. Desenvolvimento de estratégias inovadoras de imunização para viabilizar o uso de vacas como biofábricas de anticorpos neutralizantes produzidos a partir do colostro para tratamento e prevenção de doenças pandêmicas. In: WORKSHOP DE INICIAÇÃO CIENTÍFICA DA EMBRAPA GADO DE LEITE, 28., 2023, Juiz de Fora. Anais... Juiz de Fora: Embrapa Gado de Leite, 2024. p. 31-35. (Embrapa Gado de Leite. Eventos Técnicos & Científicos, 1). Pibic/Fapemig.Tipo: Artigo em Anais de Congresso |
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