Download MendeleyThe refined three-dimensional structure of 3 alpha,20 beta-hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenases.
Ghosh, D., Wawrzak, Z., Weeks, C.M., Duax, W.L., Erman, M.(1994) Structure 2: 629-640
- PubMed: 7922040
- DOI: https://doi.org/10.1016/s0969-2126(00)00064-2
- Primary Citation of Related Structures:
2HSD - PubMed Abstract:
Bacterial 3 alpha,20 beta-hydroxysteroid dehydrogenase reversibly oxidizes the 3 alpha and 20 beta hydroxyl groups of steroids derived from androstanes and pregnanes. It was the first short-chain dehydrogenase to be studied by X-ray crystallography. The previous description of the structure of this enzyme, at 2.6 A resolution, did not permit unambiguous assignment of several important groups. We have further refined the structure of the complex of the enzyme with its cofactor, nicotinamide adenine dinucleotide (NAD), and solvent molecules, at the same resolution.
Organizational Affiliation:
Medical Foundation of Buffalo, Inc., NY 14203.
