• Title of article

    The structure at 2 Å resolution of Phycocyanin from Gracilaria chilensis and the energy transfer network in a PC–PC complex Original Research Article

  • Author/Authors

    Carlos Contreras-Martel، نويسنده , , Adelio Matamala، نويسنده , , Carola Bruna، نويسنده , , German Poo-Caama?o، نويسنده , , Daniel Almonacid، نويسنده , , Maximiliano Figueroa، نويسنده , , José Mart?nez-Oyanedel، نويسنده , , Marta Bunster، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2007
  • Pages
    9
  • From page
    388
  • To page
    396
  • Abstract
    Phycocyanin is a phycobiliprotein involved in light harvesting and conduction of light to the reaction centers in cyanobacteria and red algae. The structure of C-phycocyanin from Gracilaria chilensis was solved by X-ray crystallography at 2.0 Å resolution in space group P21. An interaction model between two PC heterohexamers was built, followed by molecular dynamic refinement. The best model showed an inter-hexamer rotation of 23°. The coordinates of a PC heterohexamer (αβ)6 and of the PC–PC complex were used to perform energy transfer calculations between chromophores pairs using the fluorescence resonance energy transfer approach (FRET). Two main intra PC (Iβ382 → Iα184 → Iα584 → Iβ682 and Iβ3153 → Iβ5153) and two main inter PC (Iβ682 → IIβ382 and Iβ5153 → IIβ3153) pathways were proposed based on the values of the energy transfer constants calculated for all the chromophore pairs in the hexamer and in the complex.
  • Keywords
    protein–protein docking , structure , Phycocyanin , Gracilaria chilensis , Energy transfer pathway
  • Journal title
    Biophysical Chemistry
  • Serial Year
    2007
  • Journal title
    Biophysical Chemistry
  • Record number

    1119801