Crystal structure of yeast FAD synthetase (Fad1) in complex with FAD.
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 A 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.
Leulliot
Nicolas
N
Institut de Biochimie et de Biophysique Moléculaire et Cellulaire, CNRS-UMR8619, Université de Paris-Sud, Bât 430, 91405 Orsay Cedex, France.
Blondeau
Karine
K
Keller
Jenny
J
Ulryck
Nathalie
N
Quevillon-Cheruel
Sophie
S
van Tilbeurgh
Herman
H
D041221:Candida glabrata / Q000737:chemistry / Q000201:enzymology; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D005182:Flavin-Adenine Dinucleotide / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D009713:Nucleotidyltransferases / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000737:chemistry / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism
D029701:Saccharomyces cerevisiae Proteins; D005182:Flavin-Adenine Dinucleotide; D009713:Nucleotidyltransferases; C020143:FMN adenylyltransferase