(Q43154755)

English

Structural mechanism of signal transduction between the RNA-binding domain and the phosphotransferase system regulation domain of the LicT antiterminator.

scientific article published on 5 August 2008

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scholarly article

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11 January 2020

Structural mechanism of signal transduction between the RNA-binding domain and the phosphotransferase system regulation domain of the LicT antiterminator (English)

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11 January 2020

Hélène Déméné

1

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11 January 2020

Karine De Guillen

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11 January 2020

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Thierry Ducat

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11 January 2020

Catherine Birck

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11 January 2020

Stéphane Aymerich

5

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11 January 2020

Michel Kochoyan

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11 January 2020

Nathalie Declerck

7

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11 January 2020

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5 August 2008

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11 January 2020

Journal of Biological Chemistry

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11 January 2020

283

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11 January 2020

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11 January 2020

30838-30849

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11 January 2020

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Bacillus subtilis mutant LicT antiterminators exhibiting enzyme I- and HPr-independent antitermination affect catabolite repression of the bglPH operon

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Solution structure of the LicT-RNA antitermination complex: CAT clamping RAT.

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Sites of positive and negative regulation in the Bacillus subtilis antiterminators LicT and SacY.

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25 May 2018

Crystal structure of an activated form of the PTS regulation domain from the LicT transcriptional antiterminator

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Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data

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RNA recognition by transcriptional antiterminators of the BglG/SacY family: functional and structural comparison of the CAT domain from SacY and LicT.

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Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA

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Estimation of the number of alpha-helical and beta-strand segments in proteins using circular dichroism spectroscopy

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PRD--a protein domain involved in PTS-dependent induction and carbon catabolite repression of catabolic operons in bacteria

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Crystal structure of a new RNA-binding domain from the antiterminator protein SacY of Bacillus subtilis

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From genetic to structural characterization of a new class of RNA-binding domain within the SacY/BglG family of antiterminator proteins

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25 May 2018

LicT, a Bacillus subtilis transcriptional antiterminator protein of the BglG family

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Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation

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Regulation of the activity of the Bacillus subtilis antiterminator LicT by multiple PEP-dependent, enzyme I- and HPr-catalysed phosphorylation

1 reference

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Identifiers

10.1074/JBC.M805955200

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11 January 2020

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11 January 2020

1 reference

Europe PubMed Central

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11 January 2020

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