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Journal Article

Structure of the RBD-PRDI fragment of the antiterminator protein GlcT.

MPS-Authors
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Himmel,  S.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Wolff,  S.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Schwiegk,  C.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

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Becker,  S.
Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society;

Fulltext (public)

1542185_sup1.pdf
(Publisher version), 111KB

Supplementary Material (public)
There is no public supplementary material available
Citation

Himmel, S., Grosse, C., Wolff, S., Schwiegk, C., & Becker, S. (2012). Structure of the RBD-PRDI fragment of the antiterminator protein GlcT. Acta Crystallographica Sektion F, 68(7), 751-756. doi:10.1107/S1744309112020635.


Cite as: http://hdl.handle.net/11858/00-001M-0000-000F-EEE6-5
Abstract
GlcT 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 angstrom 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.