Fluorescence-based thermal shift data on multidrug regulator AcrR from Salmonella enterica subsp. entrica serovar Typhimurium str. LT2
The fluorescence-based thermal shift (FTS) data presented here include Table S1 and Fig. S1, and are supplemental to our original research article describing detailed structural, FTS, and fluorescence polarization analyses of the Salmonella enterica subsp. entrica serovar Typhimurium str. LT2 multidrug transcriptional regulator AcrR (StAcrR) (http://dx.doi.org/10.1016/j.jsb.2016.01.008) (Manjasetty et al., 2015 [1]). Table S1 contains chemical formulas, a Chemical Abstracts Service (CAS) Registry Number (CAS no.), FTS rank (a ligand with the highest rank) has the largest difference in the melting temperature (ΔTm), and uses as drug molecules against various pathological conditions of sixteen small-molecule ligands that increase thermal stability of StAcrR. Thermal stability of human enolase 1, a negative control protein, was not affected in the presence of various concentrations of the top six StAcrR binders (Fig. S1).
- Research Organization:
- Argonne National Laboratory (ANL), Argonne, IL (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division
- Grant/Contract Number:
- AC02-06CH11357
- OSTI ID:
- 1324834
- Alternate ID(s):
- OSTI ID: 1629106
- Journal Information:
- Data in Brief, Journal Name: Data in Brief Vol. 7 Journal Issue: C; ISSN 2352-3409
- Publisher:
- ElsevierCopyright Statement
- Country of Publication:
- United States
- Language:
- English
Loop-to-helix transition in the structure of multidrug regulator AcrR at the entrance of the drug-binding cavity
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journal | April 2016 |
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