• Title of article

    Crystal Structure of Yeast FAD Synthetase (Fad1) in Complex with FAD

  • Author/Authors

    Nicolas Leulliot، نويسنده , , Karine Blondeau، نويسنده , , Jenny Keller، نويسنده , , Nathalie Ulryck، نويسنده , , Sophie Quevillon-Cheruel، نويسنده , , Herman van Tilbeurgh، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2010
  • Pages
    6
  • From page
    641
  • To page
    646
  • Abstract
    Flavin adenine dinucleotide (FAD) synthetase is an essential enzyme responsible for the synthesis of FAD by adenylation of riboflavin monophosphate (FMN). We have solved the 1.9 Å resolution structure of Fad1, the yeast FAD synthetase, in complex with the FAD product in the active site. The structure of Fad1 shows it to be a member of the PP-ATPase superfamily. Important conformational differences in the two motifs involved in binding the phosphate moieties of FAD compared to the Candida glabrata FMNT ortholog suggests that this loop is dynamic and undergoes substantial conformational changes during its catalytic cycle.
  • Keywords
    FAD synthetase , YDL045c , PP-ATPase
  • Journal title
    Journal of Molecular Biology
  • Serial Year
    2010
  • Journal title
    Journal of Molecular Biology
  • Record number

    1251668