5zxn | pdb_00005zxn
Crystal structure of CurA from Vibrio vulnificus
Structural highlights
FunctionPublication Abstract from PubMedCurcumin 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. Structural and Biochemical Characterization of the Curcumin-Reducing Activity of CurA from Vibrio vulnificus.,Park SB, Bae DW, Clavio NAB, Zhao L, Jeong CS, Choi BM, Macalino SJY, Cha HJ, Park JB, Lee JH, Nam SJ, Choi S, Kim MK, Cha SS J Agric Food Chem. 2018 Oct 10;66(40):10608-10616. doi: 10.1021/acs.jafc.8b03647., Epub 2018 Oct 2. PMID:30251539[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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