NMR chemical shift assignment of a constitutively active fragment of the antitermination protein LicT
Author:
Funder
Agence Nationale de la Recherche
Publisher
Springer Science and Business Media LLC
Subject
Biochemistry,Structural Biology
Link
http://link.springer.com/content/pdf/10.1007/s12104-019-09914-w.pdf
Reference11 articles.
1. Déméné H, Ducat T, De Guillen K et al (2008) Structural mechanism of signal transduction between the RNA-binding domain and the phosphotransferase system regulation domain of the LicT antiterminator. J Biol Chem 283:30838–30849. https://doi.org/10.1074/jbc.M805955200
2. Ducat T, Declerck N, Kochoyan M, Déméné H (2002) 1H, 15N and 13C backbone resonance assignments of the 40 kDa LicT-CAT-PRD1 protein. J Biomol NMR 23:325–326
3. Graille M, Zhou C-Z, Receveur-Bréchot V et al (2005) Activation of the LicT transcriptional antiterminator involves a domain swing/lock mechanism provoking massive structural changes. J Biol Chem 280:14780–14789. https://doi.org/10.1074/jbc.m414642200
4. Krüger S, Hecker M (1995) Regulation of the putative bglPH operon for aryl-beta-glucoside utilization in Bacillus subtilis. J Bacteriol 177:5590–5597
5. Lindner C, Hecker M, Le Coq D, Deutscher J (2002) Bacillus subtilis mutant LicT antiterminators exhibiting enzyme I- and HPr-independent antitermination affect catabolite repression of the bglPH operon. J Bacteriol 184:4819–4828. https://doi.org/10.1128/JB.184.17.4819-4828.2002
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