Structural highlights
Function
[FAD1_YEAST] Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of yeast FAD synthetase (Fad1) in complex with FAD.,Leulliot N, Blondeau K, Keller J, Ulryck N, Quevillon-Cheruel S, van Tilbeurgh H J Mol Biol. 2010 May 21;398(5):641-6. Epub 2010 Mar 30. PMID:20359485[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Leulliot N, Blondeau K, Keller J, Ulryck N, Quevillon-Cheruel S, van Tilbeurgh H. Crystal structure of yeast FAD synthetase (Fad1) in complex with FAD. J Mol Biol. 2010 May 21;398(5):641-6. Epub 2010 Mar 30. PMID:20359485 doi:10.1016/j.jmb.2010.03.040
