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Registro Completo |
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Biblioteca(s): |
Embrapa Instrumentação. |
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Data corrente: |
09/03/2005 |
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Data da última atualização: |
09/03/2005 |
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Autoria: |
OSIRO, D.; MUNIZ, J. R. C.; COLETA FILHO, H. D.; SOUSA, A. A. S.; MACHADO, M. A.; GARRATT, R. C.; COLNAGO, L. A. |
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Título: |
Fatty acid synthesis in Xylella fastidiosa: correlations between genome studies, 13C NMR data, and molecular models. |
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Ano de publicação: |
2004 |
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Fonte/Imprenta: |
Biochemical and Biophysical Research Communications, v. 323, p. 987-995, 2004. |
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Idioma: |
Inglês |
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Conteúdo: |
Xylella fastidiosa was the first plant pathogen to have its complete genome sequence elucidated. Routine database analyses suggested that two enzymes essential for fatty acid synthesis were missing, one of these is the holo-acyl-carrier-protein synthase. However, here we demonstrate, using 13C NMR spectroscopy, that X. fastidiosa is indeed able to synthesize fatty acids from acetate via an apparently conventional metabolic pathway. We further identify a gene product HetI, an alternative phosphopantetheinyl transferase, which we propose to fill the missing link. Homology modeling of HetI shows conservation of the Coenzyme A binding site suggesting it to be an active enzyme and reveals several interesting structural features when compared with the surfactin synthase activating enzyme, on which the model was built. These include a simplified topology due to N- and C-terminal deletions and lhe observation of a novel serine ladder. |
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Palavras-Chave: |
Modelagem molecular; NMR. |
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Thesagro: |
Síntese de Proteína; Xylella Fastidiosa. |
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Categoria do assunto: |
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Marc: |
LEADER 01676naa a2200241 a 4500
001 1028851
005 2005-03-09
008 2004 bl --- 0-- u #d
100 1 $aOSIRO, D.
245 $aFatty acid synthesis in Xylella fastidiosa$bcorrelations between genome studies, 13C NMR data, and molecular models.
260 $c2004
520 $aXylella fastidiosa was the first plant pathogen to have its complete genome sequence elucidated. Routine database analyses suggested that two enzymes essential for fatty acid synthesis were missing, one of these is the holo-acyl-carrier-protein synthase. However, here we demonstrate, using 13C NMR spectroscopy, that X. fastidiosa is indeed able to synthesize fatty acids from acetate via an apparently conventional metabolic pathway. We further identify a gene product HetI, an alternative phosphopantetheinyl transferase, which we propose to fill the missing link. Homology modeling of HetI shows conservation of the Coenzyme A binding site suggesting it to be an active enzyme and reveals several interesting structural features when compared with the surfactin synthase activating enzyme, on which the model was built. These include a simplified topology due to N- and C-terminal deletions and lhe observation of a novel serine ladder.
650 $aSíntese de Proteína
650 $aXylella Fastidiosa
653 $aModelagem molecular
653 $aNMR
700 1 $aMUNIZ, J. R. C.
700 1 $aCOLETA FILHO, H. D.
700 1 $aSOUSA, A. A. S.
700 1 $aMACHADO, M. A.
700 1 $aGARRATT, R. C.
700 1 $aCOLNAGO, L. A.
773 $tBiochemical and Biophysical Research Communications$gv. 323, p. 987-995, 2004.
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Registro original: |
Embrapa Instrumentação (CNPDIA) |
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| Registros recuperados : 5 | |
| 4. |  | FORATO, L. A.; DORIGUETTO, A. C.; FISCHER, H.; MASCARENHAS, Y. P.; CRAIEVICH, A. F.; GARRATT, R. C.; COLNAGO, L. A. Conformations of Z19 and pennisetin proteins in solutin. . ACTIVIT REPORT. BRAZILIAN SYNCHROTRON LIGHT LABORATORY 2001, Campinas, p. 41-42, 2002.| Biblioteca(s): Embrapa Instrumentação. |
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| 5. | | OSIRO, D.; MUNIZ, J. R. C.; COLETA FILHO, H. D.; SOUSA, A. A. S.; MACHADO, M. A.; GARRATT, R. C.; COLNAGO, L. A. Fatty acid synthesis in Xylella fastidiosa: correlations between genome studies, 13C NMR data, and molecular models. Biochemical and Biophysical Research Communications, v. 323, p. 987-995, 2004.| Biblioteca(s): Embrapa Instrumentação. |
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| Registros recuperados : 5 | |
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