1h99

<table><tr><td colspan='2'>[[1h99]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H99 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1H99 FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LICT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1h99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h99 OCA], [http://pdbe.org/1h99 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h99 RCSB], [http://www.ebi.ac.uk/pdbsum/1h99 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1h99 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:11447120</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Vibrio subtilis ehrenberg 1835]]

[[Category: Declerck, N]]

[[Category: Tilbeurgh, H Van]]

[[Category: Transcriptional antiterminator]]