Solution structure of a C-terminal fragment (175–257) of CV_0373 protein from Chromobacterium violaceum adopts a winged helix-turn-helix (wHTH) fold
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Chromobacterium violaceum, a Gram-negative β-proteobacterium, is a species of free-living microorganisms found in soil and water. In addition to providing fundamental insights into environmental adaption strategies, genomes of these bacteria can also provide a rich source of genes with biotechnological potential and medical utility. For instance, C. violaceum produces a natural antibiotic called violaceine that has been shown to be useful for the treatment of colon and other cancers (Kodach et al. 2006). The complete genome sequence of C. violaceum was identified by the Brazilian National Genome Sequencing Consortium in 2003 (Brazilian National Genome Project 2003). Their study showed that there were 4,431 uniformly distributed predicted protein coding ORFs, and 958 (21.6 %) of these were identified as conserved hypothetical proteins. Among them, protein CV_0373 from C. violaceum(UniProtKB entry Q7P141, gi 34101683, KEGG entry cvi:CV_0373) is annotated as a...
KeywordsNOESY Spectrum Violaceine Residual Dipolar Coupling Nitrosomonas Europaea NOESY Peak List
This work was supported by the National Institute of General Medical Sciences; Protein Structure Initiative-Biology Program; Grant Number: U54-GM074958 and U54-GM094597. We thank D. Wang, C. Ciccosanti, L. Mao, H. Janjua, and T. Acton at the Rutgers protein production facility for technical support. All NMR data collection, except for RDCs, was conducted at the Ohio Biomedicine Center of Excellence in Structural Biology and Metabonomics at Miami University.
- Acton TB, Xiao R, Anderson S, Aramini J, Buchwald WA, Ciccosanti C, Conover K, Everett J, Hamilton K, Huang YJ, Janjua H, Kornhaber G, Lau J, Lee DY, Liu G, Maglaqui M, Ma L, Mao L, Patel D, Rossi P, Sahdev S, Shastry R, Swapna GV, Tang Y, Tong S, Wang D, Wang H, Zhao L, Montelione GT (2011) Preparation of protein samples for NMR structure, function, and small-molecule screening studies. Methods Enzymol 493:21–60CrossRefGoogle Scholar
- Guntert P (2004) Automated NMR structure calculation with CYANA. Methods Mol Biol 278:353–378Google Scholar
- Neri D, Szyperski T, Otting G, Senn H, Wuthrich K (1989) Stereospecific nuclear magnetic resonance assignments of the methyl groups of valine and leucine in the DNA-binding domain of the 434 repressor by biosynthetically directed fractional 13C labeling. Biochemistry 28:7510–7516CrossRefGoogle Scholar