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  • Title: Structure of NADP+-bound 7β-hydroxysteroid dehydrogenase reveals two cofactor-binding modes.
    Author: Wang R, Wu J, Jin DK, Chen Y, Lv Z, Chen Q, Miao Q, Huo X, Wang F.
    Journal: Acta Crystallogr F Struct Biol Commun; 2017 May 01; 73(Pt 5):246-252. PubMed ID: 28471355.
    Abstract:
    In mammals, bile acids/salts and their glycine and taurine conjugates are effectively recycled through enterohepatic circulation. 7β-Hydroxysteroid dehydrogenases (7β-HSDHs; EC 1.1.1.201), including that from the intestinal microbe Collinsella aerofaciens, catalyse the NADPH-dependent reversible oxidation of secondary bile-acid products to avoid potential toxicity. Here, the first structure of NADP+ bound to dimeric 7β-HSDH is presented. In one active site, NADP+ adopts a conventional binding mode similar to that displayed in related enzyme structures. However, in the other active site a unique binding mode is observed in which the orientation of the nicotinamide is different. Since 7β-HSDH has become an attractive target owing to the wide and important pharmaceutical use of its product ursodeoxycholic acid, this work provides a more detailed template to support rational protein engineering to improve the enzymatic activities of this useful biocatalyst, further improving the yield of ursodeoxycholic acid and its other applications.
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