1h99
From Proteopedia
(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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| - | [[Image:1h99.gif|left|200px]]<br /><applet load="1h99" size=" | + | [[Image:1h99.gif|left|200px]]<br /><applet load="1h99" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1h99, resolution 1.55Å" /> | caption="1h99, resolution 1.55Å" /> | ||
'''PRD OF LICT ANTITERMINATOR FROM BACILLUS SUBTILIS'''<br /> | '''PRD OF LICT ANTITERMINATOR FROM BACILLUS SUBTILIS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The transcriptional antiterminator protein LicT regulates the expression | + | 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== | ==About this Structure== | ||
| - | 1H99 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http:// | + | 1H99 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H99 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Declerck, N.]] | [[Category: Declerck, N.]] | ||
| - | [[Category: Tilbeurgh, H | + | [[Category: Tilbeurgh, H Van.]] |
[[Category: pts regulatory domain]] | [[Category: pts regulatory domain]] | ||
[[Category: transcriptional antiterminator]] | [[Category: transcriptional antiterminator]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:58:49 2008'' |
Revision as of 10:58, 21 February 2008
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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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