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| 1. |  | BALAN, A.; SANTACRUZ-PÉREZ, C.; MOUTRAN, A.; FERREIRA, L. C. S.; NESHICH, G.; BARBOSA, J. A. R. G. Crystallographic structure and substrate-binding interactions of the molybdate-binding protein of the phytopathogen Xanthomonas axonopodis pv. citri. Biochimica et Biophysica Acta, v. 1784, n. 2, p. 393-399, 2008.| Biblioteca(s): Embrapa Agricultura Digital. |
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| 2. | | OLIVEIRA, F. A.; ALVES, N.; GIACOMETTI, J. A.; CONSTANTINO, C. J. L.; MATTOSO, L. H. C.; BALAN, A. M. O. A.; JOB, A. E. Study of the thermomechanical and electrical properties of conducting composites containing natural rubber and carbon black. Journal of applied polymer science, [s. l.], v. 106, n. 2, p. 1001-1006, 2007.| Biblioteca(s): Embrapa Instrumentação. |
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| Registros recuperados : 2 | |
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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. |
Registro Completo
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Biblioteca(s): |
Embrapa Agricultura Digital. |
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Data corrente: |
16/02/2009 |
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Data da última atualização: |
15/01/2020 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Circulação/Nível: |
Internacional - A |
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Autoria: |
BALAN, A.; SANTACRUZ-PÉREZ, C.; MOUTRAN, A.; FERREIRA, L. C. S.; NESHICH, G.; BARBOSA, J. A. R. G. |
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Afiliação: |
ANDREA BALAN, USP; CAROLINA SANTACRUZ-PÉREZ, LNLS; ALEXANDRE MOUTRAN, USP; LUÍS CARLOS SOUZA FERREIRA, USP; GORAN NESHICH, CNPTIA; JOÃO ALEXANDRE RIBEIRO GONÇALVES BARBOSA, LNLS. |
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Título: |
Crystallographic structure and substrate-binding interactions of the molybdate-binding protein of the phytopathogen Xanthomonas axonopodis pv. citri. |
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Ano de publicação: |
2008 |
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Fonte/Imprenta: |
Biochimica et Biophysica Acta, v. 1784, n. 2, p. 393-399, 2008. |
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DOI: |
10.1016/j.bbapap.2007.11.013 |
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Idioma: |
Inglês |
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Conteúdo: |
In Xanthomonas axonopodis pv. citri (Xac or X. citri), the modA gene codes for a periplasmic protein (ModA) that is capable of binding molybdate and tungstate as part of the ABC-type transporter required for the uptake of micronutrients. In this study, we report the crystallographic structure of the Xac ModA protein with bound molybdate. The Xac ModA structure is similar to orthologs with known three-dimensional structures and consists of two nearly symmetrical domains separated by a hinge region where the oxyanion-binding site lies. Phylogenetic analysis of different ModA orthologs based on sequence alignments revealed three groups of molybdate-binding proteins: bacterial phytopathogens, enterobacteria and soil bacteria. Even though the ModA orthologs are segregated into different groups, the ligand-binding hydrogen bonds are mostly conserved, except for Archaeglobus fulgidus ModA. A detailed discussion of hydrophobic interactions in the active site is presented and two new residues, Ala38 and Ser151, are shown to be part of the ligand-binding pocket. |
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Palavras-Chave: |
Estrutura de cristalografia de raio-X; ModA; Molybdate-binding protein; X-ray crystal structure. |
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Thesagro: |
Proteína. |
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Thesaurus NAL: |
Xanthomonas axonopodis. |
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Categoria do assunto: |
X Pesquisa, Tecnologia e Engenharia |
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Marc: |
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001 1024588
005 2020-01-15
008 2008 bl uuuu u00u1 u #d
024 7 $a10.1016/j.bbapap.2007.11.013$2DOI
100 1 $aBALAN, A.
245 $aCrystallographic structure and substrate-binding interactions of the molybdate-binding protein of the phytopathogen Xanthomonas axonopodis pv. citri.$h[electronic resource]
260 $c2008
520 $aIn Xanthomonas axonopodis pv. citri (Xac or X. citri), the modA gene codes for a periplasmic protein (ModA) that is capable of binding molybdate and tungstate as part of the ABC-type transporter required for the uptake of micronutrients. In this study, we report the crystallographic structure of the Xac ModA protein with bound molybdate. The Xac ModA structure is similar to orthologs with known three-dimensional structures and consists of two nearly symmetrical domains separated by a hinge region where the oxyanion-binding site lies. Phylogenetic analysis of different ModA orthologs based on sequence alignments revealed three groups of molybdate-binding proteins: bacterial phytopathogens, enterobacteria and soil bacteria. Even though the ModA orthologs are segregated into different groups, the ligand-binding hydrogen bonds are mostly conserved, except for Archaeglobus fulgidus ModA. A detailed discussion of hydrophobic interactions in the active site is presented and two new residues, Ala38 and Ser151, are shown to be part of the ligand-binding pocket.
650 $aXanthomonas axonopodis
650 $aProteína
653 $aEstrutura de cristalografia de raio-X
653 $aModA
653 $aMolybdate-binding protein
653 $aX-ray crystal structure
700 1 $aSANTACRUZ-PÉREZ, C.
700 1 $aMOUTRAN, A.
700 1 $aFERREIRA, L. C. S.
700 1 $aNESHICH, G.
700 1 $aBARBOSA, J. A. R. G.
773 $tBiochimica et Biophysica Acta$gv. 1784, n. 2, p. 393-399, 2008.
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