Structural highlights
Function[GLCT_BACSU] Mediates the positive regulation of the glucose PTS operon (ptsGHI) by functioning as an antiterminator factor of transcription via its interaction with the RNA-antiterminator (RAT) sequence located upstream of the ptsG gene. The RNA-binding domain of GlcT directly binds to the RNA antiterminator (RAT) sequence and prevents transcriptional termination. GlcT binding requires two identical and nearly symmetrical triple base pairings in the RAT sequence.[1] [2] Publication Abstract from PubMedGlcT is a transcriptional antiterminator protein that is involved in regulation of glucose metabolism in Bacillus subtilis. Antiterminator proteins bind specific RNA sequences, thus preventing the formation of overlapping terminator stem-loops. The structure of a fragment (residues 3-170) comprising the RNA-binding domain (RBD) and the first regulatory domain (PRDI) of GlcT was solved at 2.0 A resolution with one molecule in the asymmetric unit. The two domains are connected by a helical linker. Their interface is mostly constituted by hydrophobic interactions. Structure of the RBD-PRDI fragment of the antiterminator protein GlcT.,Himmel S, Grosse C, Wolff S, Schwiegk C, Becker S Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Jul 1;68(Pt 7):751-6. Epub, 2012 Jun 22. PMID:22750856[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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