Structural Characterization of 1-deoxy-D-xylulose 5-phosphate Reductoisomerase From Vibrio Vulnificus

Nikita K Ussin, Anna M Bagnell, Lesa R Offermann, Rawan Abdulsalam, Makenzie L Perdue, Patrick Magee, Maksymilian Chruszcz

Biochim Biophys Acta Proteins Proteom. 2018 Dec;1866(12):1209-1215.

PMID: 30278288

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.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP551848	D-Xylulose		551-84-8	Price
AP60299436	1-Deoxy-D-xylulose		60299-43-6	Price