Cysteine-10 on 17β-Hydroxysteroid Dehydrogenase 1 Has Stabilizing Interactions in the Cofactor Binding Region and Renders Sensitivity to Sulfhydryl Modifying Chemicals
Figure 2
Position of Cys10 in wild-type 17β-HSD1 and of Ser10 in mutant 17β-HSD1. Cys10 has stabilizing interactions with neighboring residues involved directly in the binding of cofactor NADPH. A, wild-type 17β-HSD1. Cys10 has van der Waals contacts with Ile7, Gly9, Gly15, Ala34, and Thr35. Gly9, Gly15, and Thr35 contact NADP+. B, Cys10Ser mutant 17β-HSD1. Ser10 has van der Waals contacts with Ile7, Gly9, Gly15, Ala34, and Thr35. The backbone nitrogen on Gly9 and the backbone oxygen on Thr35 no longer contact the oxygen on the adenosine phosphate.
