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5KRR

1-deoxy-D-xylulose 5-phosphate reductoisomerase from Vibrio vulnificus in complex with Mn(2+)

Summary for 5KRR
Entry DOI10.2210/pdb5krr/pdb
Related5KQO 5KRV 5KRY 5KS1
Descriptor1-deoxy-D-xylulose 5-phosphate reductoisomerase, CHLORIDE ION, 1,2-ETHANEDIOL, ... (5 entities in total)
Functional Keywordsdxr 1-deoxy-d-xylulose 5-phosphate reductoisomerase, oxidoreductase
Biological sourceVibrio vulnificus (strain CMCP6)
Total number of polymer chains2
Total formula weight87637.71
Authors
Ussin, N.,Abdulsalam, R.W.,Offermann, L.R.,Perdue, M.,Chruszcz, M. (deposition date: 2016-07-07, release date: 2017-07-12, Last modification date: 2023-10-04)
Primary citationUssin, N.K.,Bagnell, A.M.,Offermann, L.R.,Abdulsalam, R.,Perdue, M.L.,Magee, P.,Chruszcz, M.
Structural characterization of 1-deoxy-D-xylulose 5-phosphate Reductoisomerase from Vibrio vulnificus.
Biochim Biophys Acta Proteins Proteom, 1866:1209-1215, 2018
Cited by
PubMed 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 Mg ions, however the Mg cations may be substituted with Mn, 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.
PubMed: 30278288
DOI: 10.1016/j.bbapap.2018.09.008
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

226707

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