Department of Chemistry, The State University of New York at Buffalo, Buffalo, NY 14260, USA.
Biochemistry. 2012 Oct 30;51(43):8475-7. doi: 10.1021/bi301171u. Epub 2012 Oct 19.
The yeast mitochondrial protein Sdh5 is required for the covalent attachment of flavin adenine dinucleotide (FAD) to protein Sdh1, a subunit of the heterotetrameric enzyme succinate dehydrogenase. The NMR structure of Sdh5 represents the first eukaryotic structure of Pfam family PF03937 and reveals a conserved surface region, which likely represents a putative Sdh1-Sdh5 interaction interface. Point mutations in this region result in the loss of covalent flavinylation of Sdh1. Moreover, chemical shift perturbation measurements showed that Sdh5 does not bind FAD in vitro, indicating that it is not a simple cofactor transporter in vivo.
酵母线粒体蛋白 Sdh5 对于黄素腺嘌呤二核苷酸（FAD）与琥珀酸脱氢酶异四聚体酶亚基 Sdh1 的共价连接是必需的。Sdh5 的 NMR 结构代表了 Pfam 家族 PF03937 的第一个真核结构，并揭示了一个保守的表面区域，该区域可能代表了 Sdh1-Sdh5 相互作用界面。该区域的点突变导致 Sdh1 的共价黄素化丧失。此外，化学位移扰动测量表明 Sdh5 不在体外结合 FAD，这表明它在体内不是一种简单的辅因子转运蛋白。
