1h99
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(New page: 200px<br /><applet load="1h99" size="450" color="white" frame="true" align="right" spinBox="true" caption="1h99, resolution 1.55Å" /> '''PRD OF LICT ANTITERM...)
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Revision as of 14:20, 20 November 2007
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PRD OF LICT ANTITERMINATOR FROM BACILLUS SUBTILIS
Overview
The transcriptional antiterminator protein LicT regulates the expression, of Bacillus subtilis operons involved in beta-glucoside metabolism. It, belongs to a newly characterized family of bacterial regulators whose, activity is controlled by the phosphoenolpyruvate:sugar phosphotransferase, system (PTS). LicT contains an N-terminal RNA-binding domain (56, residues), and a PTS regulation domain (PRD, 221 residues) that is, phosphorylated on conserved histidines in response to substrate, availability. Replacement of both His207 and His269 with a negatively, charged residue (aspartic acid) led to a highly active LicT variant that, no longer responds to either induction or catabolite repression signals, from the PTS. In contrast to wild type, the activated mutant form of the, LicT regulatory domain crystallized easily and provided the first, structure of a PRD, determined at 1.55 A resolution. The structure is a, homodimer, each monomer containing two analogous alpha-helical domains., The phosphorylation sites are totally buried at the dimer interface and, hence inaccessible to phosphorylating partners. The structure suggests, important tertiary and quaternary rearrangements upon LicT activation, which could be communicated from the protein C-terminal end up to the, RNA-binding domain.
About this Structure
1H99 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.
Reference
Crystal structure of an activated form of the PTS regulation domain from the LicT transcriptional antiterminator., van Tilbeurgh H, Le Coq D, Declerck N, EMBO J. 2001 Jul 16;20(14):3789-99. PMID:11447120
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