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
Link To Document :
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