Structural characterization of 1-deoxy-D-xylulose 5-phosphate Reductoisomerase from Vibrio vulnificus |
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| Institution: | 1. Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208, United States;2. Department of Chemistry, Davidson College, Davidson, NC 28035, United States;1. Institute of Chemical Biology and Fundamental Medicine, Siberian Branch of the Russian Academy of Sciences, Novosibirsk, Russia;2. Novosibirsk State University, Novosibirsk, Russia;1. Kusuma School of Biological Sciences, Indian Institute of Technology Delhi, India;2. Institute of Microbiology and Infection, School of Biosciences, University of Birmingham, UK;1. Molecular Biology Division, Bhabha Atomic Research Centre, Mumbai 400085, India;2. Homi Bhabha National Institute, Training School Complex, Anushakti Nagar, Mumbai 400094, India;1. State Key Laboratory of Animal Nutrition, Institute of Animal Sciences, Chinese Academy of Agricultural Sciences, Beijing 100193, PR China;2. Laboratory of Quality and Safety Risk Assessment for Dairy Products of Ministry of Agriculture, Institute of Animal Science, Chinese Academy of Agricultural Sciences, Beijing 100193, PR China;3. Key Laboratory of Quality & Safety Control for Milk and Dairy Products of Ministry of Agriculture, Institute of Animal Science, Chinese Academy of Agricultural Sciences, Beijing 100193, PR China;1. Dipartimento di Biotecnologie e Scienze della Vita, Università degli studi dell''Insubria, via J. H. Dunant 3, 21100 Varese, Italy;2. The Protein Factory, Politecnico di Milano and Università degli studi dell''Insubria, via Mancinelli 7, 20131 Milan, Italy;1. Department of Biochemistry, Universidade Estadual de Maringa, Maringa, PR 87020-900, Brazil;2. Department of Biochemistry and Molecular Biology, Universidade Federal do Parana, P.O. Box 19046, Curitiba, PR 81531-990, Brazil |
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| Abstract: | Vibrio vulnificus, a gram-negative bacterium, is the leading cause of seafood-borne illnesses and mortality in the United States. Previous studies have identified metabolites 2-C-methylerythritol 4-phosphate (MEP) as being essential for V. vulnificus growth and function. It was shown that 1-deoxy-D-xylulose-5-phosphate reductoisomerase (Dxr) is a critical enzyme in the viability of V. vulnificus, and many other bacteria, as it catalyzes the rearrangement of 1-deoxy-D-xylulose-5-phosphate (Dxp) to 2-C-methylerythritol 4-phosphate (MEP) within the MEP pathway, found in plants and bacteria. The MEP pathway produces the isoprenoids, isopentenyl diphosphate and dimethylallyl pyrophosphate. In this study, we produced and structurally characterized V. vulnificus Dxr. The enzyme forms a dimeric assembly and contains a metal ion in the active site. Protein produced in Escherichia coli co-purifies with Mg2+ ions, however the Mg2+ cations may be substituted with Mn2+, as both of these metals may be utilized by Dxrs. These findings will provide a basis for the design of Dxr inhibitors that may find application as antimicrobial compounds. |
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