5EPO

The three-dimensional structure of Clostridium absonum 7alpha-hydroxysteroid dehydrogenase

Summary for 5EPO

• Entry DOI: 10.2210/pdb5epo/pdb
• Descriptor: 7-alpha-hydroxysteroid deydrogenase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, TAUROCHENODEOXYCHOLIC ACID, ... (5 entities in total)
• Functional Keywords: oxidoreductase activity, metabolic process, oxidoreductase
• Biological source: Clostridium sardiniense
• Total number of polymer chains: 4
• Total formula weight: 118621.12

Authors

Lou, D.,Wang, B.,Wang, F. (deposition date: 2015-11-12, release date: 2016-03-23, Last modification date: 2024-03-20)

Primary citation

Lou, D.,Wang, B.,Tan, J.,Zhu, L.,Cen, X.,Ji, Q.,Wang, Y.
The three-dimensional structure of Clostridium absonum 7 alpha-hydroxysteroid dehydrogenase: new insights into the conserved arginines for NADP(H) recognition
Sci Rep, 6:22885-22885, 2016

PubMed Abstract: 7α-hydroxysteroid dehydrogenase (7α-HSDH) can catalyse the oxidation of C7 α-OH of the steroid nucleus in the bile acid metabolism. In the paper we determined the crystal structure of 7α-HSDH from Clostridium absonum (CA 7α-HSDH) complexed with taurochenodeoxycholic acid (TCDCA) and NADP(+) by X-ray diffraction, which, as a tetramer, possesses the typical α/β folding pattern. The four subunits of an asymmetric unit lie in the fact that there are the stable hydrophobic interactions between Q-axis-related subunits. Significantly, we captured an active state of the NADP(+), confirming that nicotinamide moiety of NADP(+) act as electron carrier in the dehydrogenation. On the basis of crystal structure analysis, site-directed mutagenesis and MD simulation, furthermore, we find that the guanidinium of Arg38 can form the stable cation-π interaction with the adenine ring of NADP(+), and the cation-π interaction and hydrogen bonds between Arg38 and NADP(+) have a significant anchor effect on the cofactor binding to CA 7α-HSDH.

PubMed: 26961171
DOI: 10.1038/srep22885

Experimental method

X-RAY DIFFRACTION (2 Å)