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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: |
NESHICH, I. A. P.; MORAES, F. R. de; MARANGONI, S.; MARTINS, D.; SALIM, J. A.; MAZONI, I.; MANCINI, A.; NESHICH, G.; JARDINE, J. G. |
Afiliação: |
IZABELLA AGOSTINHO PENA NESHICH, Estagiária/CNPTIA; FABIO ROGERIO DE MORAES, Bolsista/CNPTIA; S. MARANGONI, Unicamp; D. MARTINS, Unicamp; JOSÉ AUGUSTO SALIM, Estagiário/CNPTIA; IVAN MAZONI, CNPTIA; ADAUTO LUIZ MANCINI, CNPTIA; GORAN NESHICH, CNPTIA; JOSE GILBERTO JARDINE, CNPTIA. |
Título: |
Xylella fastidiosa hexameric pilus retraction motor PILT interfaces are maintained by non-hydrophobic contacts. |
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: |
Xylella fastidiosa (Xf) causes CVC and Pierce?s Disease (affecting citrus and grape). Xf colonizes the xylem vessels in plants. Pathogenicity of the Xf are related to ability to move within the xylem. Avirulent strains rarely move from the inoculation point. Xf has proteins involved in type IV pili, which cause the twitching motility - a form of surface-associated movement. Satyshur and coworkers had solved four structures from PilT proteins (PDB codes: 2GSZ, 2EWV, 2EWW and 2EYU) from a hyperthermophilic organism, Aquifex aeolicus (Aa). PilT is a hexameric ATPase from a subgroup of the bacterial type II/type IV secretion systems, with two major domains: the Nterminal Domain (NTD) and the C-Terminal Domain (CTD) which contains the ATPase core. The importance of polar and charged CTDn: NTDn+1 interface interactions to retraction motion was discussed. Through site-directed mutagenesis on Pseudomonas aeruginosa PilT, they demonstrated that some residues are crucial to protein function, half of them (D29, R95 and R207) located on interface region. The Xf PilT has 68% of similarity and 49% of identical aminoacids to Aa). We modelled each Xf PilT chain. We analyzed the hexameric structure of Aa Pilt (PDB code: 2GSZ) and Xf PilT hexamer model (named here as 2HXF) using Blue Star STING platform. By analysis of Interface Forming Residues (IFR), we found that there was a significant difference among the interfaces: Xf PilT interfaces area occupied mainly by charged amino acids. This does not hold for the free surfaces (molecular surface without interfaces). In 2GSZ the interface area is occupied by hydrophobic and polar AA; In addition, the interfaces have less charged AA than free surface. The Aa PilT interfaces are more hydrophobic when compared to Xf PilT. The number and energies of contacts established between IFRs in 2HXF are higher than 2GSZ, suggesting that Xf PilT interfaces are more stable. Apparently, the most important IFRs (which establish most energetic contacts at the surface) are conserved within Proteobacteria and Aquificae PilTs (Clustalw alignment data). Thus, we suggest that the difference among amino acid composition of interfaces between Xf PilT and Aa PilT reflect their crucial importance on successful host infections across the Proteobacteria. We hypothesize here that similarities found in primary sequence alignment could be maintained at 3D level, indicating a possible higher selective pressure on these locations in Proteobacteria (as compared to the Aa PilT). We also suggest that these residues, crucially important to protein functionality, might serve as potential targets to eliminate bacteria pathogenicity. MenosXylella fastidiosa (Xf) causes CVC and Pierce?s Disease (affecting citrus and grape). Xf colonizes the xylem vessels in plants. Pathogenicity of the Xf are related to ability to move within the xylem. Avirulent strains rarely move from the inoculation point. Xf has proteins involved in type IV pili, which cause the twitching motility - a form of surface-associated movement. Satyshur and coworkers had solved four structures from PilT proteins (PDB codes: 2GSZ, 2EWV, 2EWW and 2EYU) from a hyperthermophilic organism, Aquifex aeolicus (Aa). PilT is a hexameric ATPase from a subgroup of the bacterial type II/type IV secretion systems, with two major domains: the Nterminal Domain (NTD) and the C-Terminal Domain (CTD) which contains the ATPase core. The importance of polar and charged CTDn: NTDn+1 interface interactions to retraction motion was discussed. Through site-directed mutagenesis on Pseudomonas aeruginosa PilT, they demonstrated that some residues are crucial to protein function, half of them (D29, R95 and R207) located on interface region. The Xf PilT has 68% of similarity and 49% of identical aminoacids to Aa). We modelled each Xf PilT chain. We analyzed the hexameric structure of Aa Pilt (PDB code: 2GSZ) and Xf PilT hexamer model (named here as 2HXF) using Blue Star STING platform. By analysis of Interface Forming Residues (IFR), we found that there was a significant difference among the interfaces: Xf PilT interfaces area occupied mainly by charged amino acids. This do... Mostrar Tudo |
Palavras-Chave: |
Aminoácidos; Bioinformática; Contatos não hidrofóbicos; Proteínas. |
Thesagro: |
Xylella Fastidiosa. |
Thesaurus Nal: |
Bioinformatics; Proteins. |
Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
Marc: |
LEADER 03706nam a2200313 a 4500 001 1576270 005 2020-01-15 008 2009 bl uuuu u00u1 u #d 100 1 $aNESHICH, I. A. P. 245 $aXylella fastidiosa hexameric pilus retraction motor PILT interfaces are maintained by non-hydrophobic contacts.$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 $aXylella fastidiosa (Xf) causes CVC and Pierce?s Disease (affecting citrus and grape). Xf colonizes the xylem vessels in plants. Pathogenicity of the Xf are related to ability to move within the xylem. Avirulent strains rarely move from the inoculation point. Xf has proteins involved in type IV pili, which cause the twitching motility - a form of surface-associated movement. Satyshur and coworkers had solved four structures from PilT proteins (PDB codes: 2GSZ, 2EWV, 2EWW and 2EYU) from a hyperthermophilic organism, Aquifex aeolicus (Aa). PilT is a hexameric ATPase from a subgroup of the bacterial type II/type IV secretion systems, with two major domains: the Nterminal Domain (NTD) and the C-Terminal Domain (CTD) which contains the ATPase core. The importance of polar and charged CTDn: NTDn+1 interface interactions to retraction motion was discussed. Through site-directed mutagenesis on Pseudomonas aeruginosa PilT, they demonstrated that some residues are crucial to protein function, half of them (D29, R95 and R207) located on interface region. The Xf PilT has 68% of similarity and 49% of identical aminoacids to Aa). We modelled each Xf PilT chain. We analyzed the hexameric structure of Aa Pilt (PDB code: 2GSZ) and Xf PilT hexamer model (named here as 2HXF) using Blue Star STING platform. By analysis of Interface Forming Residues (IFR), we found that there was a significant difference among the interfaces: Xf PilT interfaces area occupied mainly by charged amino acids. This does not hold for the free surfaces (molecular surface without interfaces). In 2GSZ the interface area is occupied by hydrophobic and polar AA; In addition, the interfaces have less charged AA than free surface. The Aa PilT interfaces are more hydrophobic when compared to Xf PilT. The number and energies of contacts established between IFRs in 2HXF are higher than 2GSZ, suggesting that Xf PilT interfaces are more stable. Apparently, the most important IFRs (which establish most energetic contacts at the surface) are conserved within Proteobacteria and Aquificae PilTs (Clustalw alignment data). Thus, we suggest that the difference among amino acid composition of interfaces between Xf PilT and Aa PilT reflect their crucial importance on successful host infections across the Proteobacteria. We hypothesize here that similarities found in primary sequence alignment could be maintained at 3D level, indicating a possible higher selective pressure on these locations in Proteobacteria (as compared to the Aa PilT). We also suggest that these residues, crucially important to protein functionality, might serve as potential targets to eliminate bacteria pathogenicity. 650 $aBioinformatics 650 $aProteins 650 $aXylella Fastidiosa 653 $aAminoácidos 653 $aBioinformática 653 $aContatos não hidrofóbicos 653 $aProteínas 700 1 $aMORAES, F. R. de 700 1 $aMARANGONI, S. 700 1 $aMARTINS, D. 700 1 $aSALIM, J. A. 700 1 $aMAZONI, I. 700 1 $aMANCINI, A. 700 1 $aNESHICH, G. 700 1 $aJARDINE, J. G.
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Embrapa Agricultura Digital (CNPTIA) |
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Registros recuperados : 21 | |
2. | | NESHICH, I. A. P.; MORAES, F. R. de; SALIM, J. A.; MAZONI, I.; MANCINI, A.; JARDINE, J. G.; NESHICH, G. Surface hydrophobicity index (SHI): insight into the mechanisms of protein-protein associations. In: INTERNATIONAL CONFERENCE OF THE BRAZILIAN ASSOCIATION FOR BIOINFORMATICS AND COMPUTATIONAL BIOLOGY, 5., 2009, Angra dos Reis. Abstracts book... Angra dos Reis: ABBCB, 2009. Não paginado. X-Meeting 2009Tipo: Resumo em Anais de Congresso |
Biblioteca(s): Embrapa Agricultura Digital. |
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3. | | MAZONI, I.; SALIM, J. A; NESHICH, I. A. P.; MORAES, F. R. de; NISHIMURA, L.; JARDINE, J. G.; NESHICH, G. Structure function relationship de convoluted to a level of physical chemical descriptors: case study - lysozyme / lactalbumine differences. In: ANNUAL MEETING OF THE SBBq, 40., 2011, Foz do Iguaçu. [Proceedings...]. São Paulo, SP: Brazilian Society for Biochemistry and Molecular Biology, 2011. Não paginado.Tipo: Resumo em Anais de Congresso |
Biblioteca(s): Embrapa Agricultura Digital. |
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4. | | NESHICH, I. A. P.; MORAES, F. de; SALIM, J. A.; MAZONI, I.; JARDINE, J. G.; NESHICH, G. Size matters: surface hydrophobicity index (SHI) describes the impact of the size of interface area on oligomerization driven by hydrophobic effect. In: ANNUAL INTERNATIONAL CONFERENCE ON INTELLIGENT SYSTEMS FOR MOLECULAR BIOLOGY; STRUCTURAL BIOINFORMATICS AND COMPUTATIONAL BIOPHYSICS MEETING, 8., 2012, Long Beach, California. Abstracts... California: ISMB, 2012. Não paginado. 3Dsig 2012.Tipo: Resumo em Anais de Congresso |
Biblioteca(s): Embrapa Agricultura Digital. |
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5. | | NESHICH, I. A. P.; MAZONI, I.; SALIM, J. A.; MORAES, F. R. de; NISHIMURA, L.; JARDINE, J. G.; NESHICH, G. Pathogenic Prion Proteins (PrP) have higher electrostatic potential pattern than normal cellular prion protein in a specific region. In: ANNUAL MEETING OF THE SBBq, 40., 2011, Foz do Iguaçu. [Proceedings...]. São Paulo, SP: Brazilian Society for Biochemistry and Molecular Biology, 2011. Não paginado.Tipo: Resumo em Anais de Congresso |
Biblioteca(s): Embrapa Agricultura Digital. |
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6. | | JARDINE, J. G.; NESHICH, I. A. P.; MORAES, F. R. de; MAZONI, I.; MANCINI, A.; SALIM, J. A.; NESHICH, G. Generation of lipase B mutants with increased surface hydrophobicity in order to improve biodiesel catalysis. In: INTERNATIONAL CONFERENCE OF THE BRAZILIAN ASSOCIATION FOR BIOINFORMATICS AND COMPUTATIONAL BIOLOGY, 5., 2009, Angra dos Reis. Abstracts book... Angra dos Reis: ABBCB, 2009. Não paginado. X-Meeting 2009.Tipo: Resumo em Anais de Congresso |
Biblioteca(s): Embrapa Agricultura Digital. |
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7. | | JARDINE, J. G.; NESHICH, I. A. P.; MAZONI, I.; YANO, I. H.; MORAES, F. R. de; SALIM, J. A.; BORRO, L.; NISHIMURA, L. S.; NESHICH, G. Biologia computacional molecular e suas aplicações na agricultura. In: MASSRUHÁ, S. M. F. S.; LEITE, M. A. de A.; LUCHIARI JUNIOR, A.; ROMANI, L. A. S. (Ed.). Tecnologias da informação e comunicação e suas relações com a agricultura. Brasília, DF: Embrapa, 2014. Cap. 6. p. 101-117.Tipo: Capítulo em Livro Técnico-Científico |
Biblioteca(s): Embrapa Agricultura Digital. |
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8. | | DIAS-LOPES, C.; NESHICH, I. A. P.; NESHICH, G.; ORTEGA, J. M.; GRANIER, C.; CHÁVEZ-OLORTEGUI, C.; MOLINA, F.; FELICORI, L. Identification of new Sphingomyelinases D in pathogenic fungi and other pathogenic organisms. PLoS ONE, San Francisco, v. 8, n. 11, p. 1-12, 2013.Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 1 |
Biblioteca(s): Embrapa Agricultura Digital. |
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9. | | MORAES, F. R. de; NESHICH, I. A. P.; MAZONI, I.; YANO, I. H.; PEREIRA, J. G. C.; SALIM, J. A.; JARDINE, J. G.; NESHICH, G. Improving predictions of protein-protein interfaces by combining amino acid-specific classifiers based on structural and physicochemical descriptors with their weighted neighbor averages. Plos One, San Francisco, v. 9, n. 1, p. 1-15, Jan. 2014.Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 1 |
Biblioteca(s): Embrapa Agricultura Digital. |
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10. | | SALIM, J. A.; VON ZUBEN, F. J.; MORAES, F. R. de; NESHICH, I. A. P.; MAZONI, I.; JARDINE, J.; NESHICH, G. Characterization of catalytic site residues using STING_DB structural descriptors. In: ANNUAL INTERNATIONAL CONFERENCE ON INTELLIGENT SYSTEMS FOR MOLECULAR BIOLOGY; STRUCTURAL BIOINFORMATICS AND COMPUTATIONAL BIOPHYSICS CONFERENCE MEETING, 8., 2012, Long Beach, California. Abstracts... California: ISCB, 2012. Não paginado. Poster. 3DSIG 2012.Tipo: Resumo em Anais de Congresso |
Biblioteca(s): Embrapa Agricultura Digital. |
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11. | | MAZONI, I.; BORRO, L. C.; MANCINI, A.; SALIM, J. A.; MORAES, F. R.; JARDINE, J. G.; NESHICH, I. A. P.; NESHICH, G. Comparison between physical chemical and geometrical characteristics of the amino acids present in alpha-helices and beta-sheets. In: INTERNATIONAL CONFERENCE OF THE BRAZILIAN ASSOCIATION FOR BIOINFORMATICS AND COMPUTATIONAL BIOLOGY, 5., 2009, Angra dos Reis. Abstracts book... Angra dos Reis: ABBCB, 2009. Não pagiando. X-Meeting 2009.Tipo: Resumo em Anais de Congresso |
Biblioteca(s): Embrapa Agricultura Digital. |
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12. | | JARDINE, J. G.; NESHICH, I. A. P.; MAZONI, I.; YANO, I. H.; MORAES, F. R. de; SALIM, J. A; BORRO, L.; NISHIMURA, L. S.; NESHICH, G. Computational Molecular Biology and its applications in agriculture. In: MASSRUHÁ, S. M. F. S.; LEITE, M. A. de A.; LUCHIARI JUNIOR, A.; ROMANI, L. A. S. (Ed.). Information and communication technologies and their relations with agriculture. Brasília, DF: Embrapa, 2016. ch. 6, p. 103-118.Tipo: Capítulo em Livro Técnico-Científico |
Biblioteca(s): Embrapa Agricultura Digital. |
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13. | | NESHICH, G.; NESHICH, I. A. P.; MORAES, F.; SALIM, J. A.; BORRO, L.; YANO, I. H.; MAZONI, I.; JARDINE, J. G.; ROCCHIA, W. Using structural and physical-chemical parameters to identify, classify, and predict functional districts in proteins-the role of electrostatic potential. In: ROCCHIA, W.; SPAGNUOLO, M. (Ed.). Computational electrostatics for biological applications: geometric and numerical approaches to the description of electrostatic interaction between macromolecules. Cham: Springer, 2015. Chapter 12. p. 227-254.Tipo: Capítulo em Livro Técnico-Científico |
Biblioteca(s): Embrapa Agricultura Digital. |
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15. | | MORAES, F. R. de; VILLANUEVA, W. J. P.; NESHICH, I. A. P.; MAZONI, I.; NISHIMURA, L.; SALIM, J. A.; JARDINE, J. G.; VON ZUBEN, F.; NESHICH, G. SIPEPPI, a systematic neuron network-based methodology for predicting protein-protein interfaces using STING database descriptors. In: ANNUAL MEETING OF THE SBBq, 40., 2011, Foz do Iguaçu. [Proceedings...]. São Paulo, SP: Brazilian Society for Biochemistry and Molecular Biology, 2011. Não paginado.Tipo: Resumo em Anais de Congresso |
Biblioteca(s): Embrapa Agricultura Digital. |
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16. | | BRAGHINI, C. A.; NESHICH, I. A. P.; NESHICH, G.; SOARDI, F. C.; MELLO, M. P. de; COSTA, V. P.; VASCONCELLOS, J. P. C. de; MELO, M. B. de. New mutation in the myocilin gene segregates with juvenile-onset open-angle glaucoma in a Brazilian family Gene, Amsterdam, v. 535, n. 1, p. 50-57, July 2013.Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 2 |
Biblioteca(s): Embrapa Agricultura Digital. |
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17. | | SALIM, J. A.; MORAES, F. R. de; NESHICH, I. A. P.; MAZONI, I.; JARDINE, J. G.; VON ZUBEN, F.; NESHICH, G. A pattern recognition approach for catalytic site residues prediction using STING structural protein descriptors. In: REUNIÃO ANUAL DA SOCIEDADE BRASILEIRA DE BIOQUÍMICA E BIOLOGIA MOLECULAR, 41., 2012, Foz do Iguaçu. Resumos... [S.l]: SBBq, 2012. Não paginado. 1 pôster.Tipo: Resumo em Anais de Congresso |
Biblioteca(s): Embrapa Agricultura Digital. |
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18. | | NESHICH, I. A. P.; MORAES, F. R. de; MARANGONI, S.; MARTINS, D.; SALIM, J. A.; MAZONI, I.; MANCINI, A.; NESHICH, G.; JARDINE, J. G. Xylella fastidiosa hexameric pilus retraction motor PILT interfaces are maintained by non-hydrophobic contacts. In: INTERNATIONAL CONFERENCE OF THE BRAZILIAN ASSOCIATION FOR BIOINFORMATICS AND COMPUTATIONAL BIOLOGY, 5., 2009, Angra dos Reis. Abstracts book... Angra dos Reis: ABBCB, 2009. Não paginado. X-Meeting 2009.Tipo: Resumo em Anais de Congresso |
Biblioteca(s): Embrapa Agricultura Digital. |
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19. | | RIBEIRO, C.; TOGAWA, R. C.; NESHICH, I. A. P.; MAZONI, I.; MANCINI, A. L.; MINARDI, R. C. de M.; SILVEIRA, C. H. da; JARDINE, J. G.; SANTORO, M. M.; NESHICH, G. Analysis of binding properties and specificity through identification of the interface forming residues (IFR) for serine proteases in silico docked to different inhibitors. BMC Structural Biology, London, v. 10, n. 36, p. 1-16, 2010.Tipo: Artigo em Periódico Indexado | Circulação/Nível: B - 1 |
Biblioteca(s): Embrapa Agricultura Digital. |
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20. | | RIBEIRO; TOGAWA, R. C.; NESHICH, I. A. P.; MAZONI, I.; MANCINI, A. L.; MINARDI, R. C. de M.; SILVEIRA, C. H. da; JARDINE, J. G.; SANTORO, M. M.; NESHICH, G. Analysis of binding properties and specificity through identification of the interface forming residues (IFR) for serine proteases in silico docked to different inhibitors. BMC Structural Biology, London, v. 10, n. 36, p. 1-16, 2010. Disponível em:.Acesso em: 5 jan. 2011.Tipo: Artigo em Periódico Indexado | Circulação/Nível: B - 1 |
Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
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Registros recuperados : 21 | |
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Nenhum registro encontrado para a expressão de busca informada. |
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