5ZXU

Crystal structure of CurA in complex with NADPH from Vibrio vulnificus

Summary for 5ZXU

• Entry DOI: 10.2210/pdb5zxu/pdb
• Related: 5ZXN
• Descriptor: NADP-dependent oxidoreductase, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• Functional Keywords: reductase, oxidoreductase
• Biological source: Vibrio vulnificus MO6-24/O
• Total number of polymer chains: 1
• Total formula weight: 37185.08

Authors

Kim, M.-K.,Bae, D.-W.,Cha, S.-S. (deposition date: 2018-05-21, release date: 2019-04-03, Last modification date: 2023-11-22)

Primary citation

Park, S.B.,Bae, D.W.,Clavio, N.A.B.,Zhao, L.,Jeong, C.S.,Choi, B.M.,Macalino, S.J.Y.,Cha, H.J.,Park, J.B.,Lee, J.H.,Nam, S.J.,Choi, S.,Kim, M.K.,Cha, S.S.
Structural and Biochemical Characterization of the Curcumin-Reducing Activity of CurA from Vibrio vulnificus.
J. Agric. Food Chem., 66:10608-10616, 2018

PubMed Abstract: Curcumin is a yellow-colored ingredient in dietary spice turmeric ( Curcuma longa Linn). This nontoxic polyphenol has antitumor, anti-inflammatory, apoptotic, and antioxidant activities. The ingested curcumin is reduced to multihydrated forms with more potent therapeutic potentials by the curcumin reductase (CurA) from commensal Escherichia coli. In this study, we demonstrated that Vibrio vulnificus CurA ( VvCurA) with 87% sequence similarity to the E. coli CurA exhibits the curcumin-reducing activity through spectrophotometric detection of NADPH oxidation and high performance liquid chromatographic analysis of curcumin consumption and product generation. Afterward, we determined the crystal structures of VvCurA and the VvCurA/NADPH complex, and made the in silico model of the VvCurA/NADPH/curcumin ternary complex through induced fit docking. Based on structural information, active site residues that play critical roles in catalysis have been identified and characterized by mutational and kinetic studies, leading us to propose the reaction mechanism of CurA.

PubMed: 30251539
DOI: 10.1021/acs.jafc.8b03647

Experimental method

X-RAY DIFFRACTION (2.2 Å)