Computer-Based Annotation of Putative AraC/XylS-Family Transcription Factors of Known Structure but Unknown Function.

Currently, about 20 crystal structures per day are released and deposited in the Protein Data Bank. A significant fraction of these structures is produced by research groups associated with the structural genomics consortium. The biological function of many of these proteins is generally unknown or...

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Publicado en:Journal of Biomedicine & Biotechnology Vol. 2012; pp. 1 - 15
Autores principales: Schüller, Andreas, Slater, Alex W., Norambuena, Tomás, Cifuentes, Juan J., Almonacid, Leonardo I., Melo, Francisco
Formato: pictorial research tables/charts Journal Article
Publicado: Wiley-Blackwell 2012
Acceso en línea:Ver este registro en EBSCOhost
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      dt: 2012
      vid: 2012
      pid: 480
      pub: Wiley-Blackwell
      place: Malden, Massachusetts
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        atl: Computer-Based Annotation of Putative AraC/XylS-Family Transcription Factors of Known Structure but Unknown Function.
      aug:
        au:
          Schüller, Andreas
          Slater, Alex W.
          Norambuena, Tomás
          Cifuentes, Juan J.
          Almonacid, Leonardo I.
          Melo, Francisco
        affil: Molecular Bioinformatics Laboratory, Millennium Institute on Immunology and Immunotherapy, Departamento de Genética Molecular y Microbiología, Facultad de Ciencias Biológicas, Pontificia Universidad Católica de Chile, Alameda 340, 8331150 Santiago, Chile
      sug:
        subj:
          Bioinformatics Methods
          Proteins Classification
          Resource Databases
          Proteins Physiology
          Bacteria Analysis
          Genomics
          Amino Acids
          Binding Sites
          Cluster Analysis
          Models, Theoretical
          Models, Statistical
          Models, Structural
          Data Analysis Software
          Sequence Analysis
          Human
          Funding Source
      ab: Currently, about 20 crystal structures per day are released and deposited in the Protein Data Bank. A significant fraction of these structures is produced by research groups associated with the structural genomics consortium. The biological function of many of these proteins is generally unknown or not validated by experiment. Therefore, a growing need for functional prediction of protein structures has emerged. Here we present an integrated bioinformatics method that combines sequence-based relationships and three-dimensional (3D) structural similarity of transcriptional regulators with computer prediction of their cognate DNA binding sequences. We applied this method to the AraC/XylS family of transcription factors, which is a large family of transcriptional regulators found in many bacteria controlling the expression of genes involved in diverse biological functions. Three putative new members of this family with known 3D structure but unknown function were identified for which a probable functional classification is provided. Our bioinformatics analyses suggest that they could be involved in plant cell wall degradation (Lin2118 protein from Listeria innocua, PDB code 3oou), symbiotic nitrogen fixation (protein from Chromobacterium violaceum, PDB code 3oio), and either metabolism of plant-derived biomass or nitrogen fixation (protein from Rhodopseudomonas palustris, PDB code 3mn2).
      pubtype: Academic Journal
      doctype:
        pictorial
        research
        tables/charts
        Journal Article
      ougenre: Article
    language: English
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