3WCZ

Crystal structure of Bombyx mori aldo-keto reductase (AKR2E4) in complex with NADP

Summary for 3WCZ

• Entry DOI: 10.2210/pdb3wcz/pdb
• Descriptor: Aldo-keto reductase 2E, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, 1,2-ETHANEDIOL, ... (5 entities in total)
• Functional Keywords: tim-barrel, reductase, nadp, cytosol, oxidoreductase
• Biological source: Bombyx mori (silk moth,silkworm)
• Total number of polymer chains: 1
• Total formula weight: 35569.45

Authors

Yamamoto, K.,Wilson, D.K. (deposition date: 2013-06-05, release date: 2014-01-01, Last modification date: 2023-11-08)

Primary citation

Yamamoto, K.,Wilson, D.K.
Identification, characterization, and crystal structure of an aldo-keto reductase (AKR2E4) from the silkworm Bombyx mori.
Arch.Biochem.Biophys., 538:156-163, 2013

PubMed Abstract: A new member of the aldo-keto reductase (AKR) superfamily with 3-dehydroecdysone reductase activity was found in the silkworm Bombyx mori upon induction by the insecticide diazinon. The amino acid sequence showed that this enzyme belongs to the AKR2 family, and the protein was assigned the systematic name AKR2E4. In this study, recombinant AKR2E4 was expressed, purified to near homogeneity, and kinetically characterized. Additionally, its ternary structure in complex with NADP(+) and citrate was refined at 1.3Å resolution to elucidate substrate binding and catalysis. The enzyme is a 33-kDa monomer and reduces dicarbonyl compounds such as isatin and 17α-hydroxy progesterone using NADPH as a cosubstrate. No NADH-dependent activity was detected. Robust activity toward the substrate inhibitor 3-dehydroecdysone was observed, which suggests that this enzyme plays a role in regulation of the important molting hormone ecdysone. This structure constitutes the first insect AKR structure determined. Bound NADPH is located at the center of the TIM- or (β/α)8-barrel, and residues involved in catalysis are conserved.

PubMed: 24012638
DOI: 10.1016/j.abb.2013.08.018

Experimental method

X-RAY DIFFRACTION (1.3 Å)