Institut de Biochimie et de Biophysique Moléculaire et Cellulaire, CNRS-UMR8619, Université de Paris-Sud, Bât 430, 91405 Orsay Cedex, France.
J Mol Biol. 2010 May 21;398(5):641-6. doi: 10.1016/j.jmb.2010.03.040. Epub 2010 Mar 30.
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.
黄素腺嘌呤二核苷酸(FAD)合成酶是一种必需的酶,负责通过将核黄素单磷酸(FMN)腺苷酸化来合成 FAD。我们已经解决了 Fad1(酵母 FAD 合成酶)与活性位点中 FAD 产物结合的 1.9 A 分辨率结构。Fad1 的结构表明它是 PP-ATPase 超家族的成员。与 Candida glabrata FMNT 同源物相比,FAD 磷酸部分结合的两个模体中的重要构象差异表明该环是动态的,并且在其催化循环中经历了很大的构象变化。