7VEM

the NADPH-assisted quinone oxidoreductase from Phytophthora capsici

Summary for 7VEM

• Entry DOI: 10.2210/pdb7vem/pdb
• Descriptor: the NADPH-assisted quinone oxidoreductase, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: nadph, quinone oxidoreductase, phytophthora capsici, protein binding
• Biological source: Phytophthora capsici LT1534
• Total number of polymer chains: 2
• Total formula weight: 76215.91

Authors

Yang, C.C.,Zhu, C.Y. (deposition date: 2021-09-09, release date: 2021-11-10, Last modification date: 2024-05-29)

Primary citation

Yang, C.,Huang, Z.,Zhang, X.,Zhu, C.
Structural Insights into the NAD(P)H:Quinone Oxidoreductase from Phytophthora capsici.
Acs Omega, 7:25705-25714, 2022

PubMed Abstract: Soluble quinone oxidoreductases catalyze transfer of electrons from NADPH to quinones. Transfer of electrons is essential for detoxification of synthetic compounds. Here, we present the crystal structure of a NADPH-dependent QOR from () complexed with NADPH at 2.4 Å resolution. The enzyme exhibits a bi-modular architecture, containing a NADPH-binding groove and a substrate-binding pocket in each subunit. In the crystal, each asymmetric unit of QOR contains two molecules stabilized by intermolecular interactions. Gel filtration and ultracentrifugation analyses reveal that it functions as a tetramer in solution. Alignment of homologous structures exhibits a conserved topology. However, the active sites vary among the homologues, indicating differences in substrate specificities. Enzymatic assays indicate that QOR tends to catalyze the large substrates, like 9,10-phenanthrenequinone. Computational simulation associated with site-directed mutagenesis and enzymatic activity analysis declares a potential quinone-binding channel. The ability to reduce quinones probably helps to detoxify some harmful chemicals encountered during invasion.

PubMed: 35910145
DOI: 10.1021/acsomega.2c02954

Experimental method

X-RAY DIFFRACTION (2.39 Å)