5FYD

Structural and biochemical insights into 7beta-hydroxysteroid dehydrogenase stereoselectivity

Summary for 5FYD

• Entry DOI: 10.2210/pdb5fyd/pdb
• Descriptor: OXIDOREDUCTASE, SHORT CHAIN DEHYDROGENASE/REDUCTASE FAMILY PROTEIN, GLYCEROL (3 entities in total)
• Functional Keywords: oxidoreductase, short-chain dehydrogenase, steroid, stereoselectivity, dehydrogenase
• Biological source: COLLINSELLA AEROFACIENS
• Total number of polymer chains: 2
• Total formula weight: 57659.65

Authors

Savino, S.,Ferrandi, E.,Forneris, F.,Rovida, S.,Riva, S.,Monti, D.,Mattevi, A. (deposition date: 2016-03-07, release date: 2016-04-06, Last modification date: 2024-01-10)

Primary citation

Savino, S.,Ferrandi, E.E.,Forneris, F.,Rovida, S.,Riva, S.,Monti, D.,Mattevi, A.
Structural and Biochemical Insights Into 7Beta-Hydroxysteroid Dehydrogenase Stereoselectivity.
Proteins, 84:859-, 2016

PubMed Abstract: Hydroxysteroid dehydrogenases are of great interest as biocatalysts for transformations involving steroid substrates. They feature a high degree of stereo- and regio-selectivity, acting on a defined atom with a specific configuration of the steroid nucleus. The crystal structure of 7β-hydroxysteroid dehydrogenase from Collinsella aerofaciens reveals a loop gating active-site accessibility, the bases of the specificity for NADP(+) , and the general architecture of the steroid binding site. Comparison with 7α-hydroxysteroid dehydrogenase provides a rationale for the opposite stereoselectivity. The presence of a C-terminal extension reshapes the substrate site of the β-selective enzyme, possibly leading to an inverted orientation of the bound substrate. Proteins 2016; 84:859-865. © 2016 Wiley Periodicals, Inc.

PubMed: 27006087
DOI: 10.1002/PROT.25036

Experimental method

X-RAY DIFFRACTION (1.6 Å)