1HXH

COMAMONAS TESTOSTERONI 3BETA/17BETA HYDROXYSTEROID DEHYDROGENASE

Summary for 1HXH

• Entry DOI: 10.2210/pdb1hxh/pdb
• Related: 2hsd
• Descriptor: 3BETA/17BETA-HYDROXYSTEROID DEHYDROGENASE (2 entities in total)
• Functional Keywords: alpha-beta, rossmann fold, short-chain dehydrogenase, oxidoreductase
• Biological source: Comamonas testosteroni
• Total number of polymer chains: 4
• Total formula weight: 107391.42

Authors

Benach, J.,Filling, C.,Oppermann, U.C.T.,Roversi, P.,Bricogne, G.,Berndt, K.D.,Jornvall, H.,Ladenstein, R. (deposition date: 2001-01-15, release date: 2002-12-25, Last modification date: 2023-08-09)

Primary citation

Benach, J.,Filling, C.,Oppermann, U.C.T.,Roversi, P.,Bricogne, G.,Berndt, K.D.,Jornvall, H.,Ladenstein, R.
Structure of Bacterial 3beta/17beta-Hydroxysteroid Dehydrogenase at 1.2 A Resolution: A Model for Multiple Steroid Recognition
Biochemistry, 41:14659-14668, 2002

PubMed Abstract: The enzyme 3beta/17beta-hydroxysteroid dehydrogenase (3beta/17beta-HSD) is a steroid-inducible component of the Gram-negative bacterium Comamonas testosteroni. It catalyzes the reversible reduction/dehydrogenation of the oxo/beta-hydroxy groups at positions 3 and 17 of steroid compounds, including hormones and isobile acids. Crystallographic analysis at 1.2 A resolution reveals the enzyme to have nearly identical subunits that form a tetramer with 222 symmetry. This is one of the largest oligomeric structures refined at this resolution. The subunit consists of a monomer with a single-domain structure built around a seven-stranded beta-sheet flanked by six alpha-helices. The active site contains a Ser-Tyr-Lys triad, typical for short-chain dehydrogenases/reductases (SDR). Despite their highly diverse substrate specificities, SDR members show a close to identical folding pattern architectures and a common catalytic mechanism. In contrast to other SDR apostructures determined, the substrate binding loop is well-defined. Analysis of structure-activity relationships of catalytic cleft residues, docking analysis of substrates and inhibitors, and accessible surface analysis explains how 3beta/17beta-HSD accommodates steroid substrates of different conformations.

PubMed: 12475215
DOI: 10.1021/bi0203684

Experimental method

X-RAY DIFFRACTION (1.22 Å)