1rzr
From Proteopedia
(New page: 200px<br /><applet load="1rzr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rzr, resolution 2.80Å" /> '''crystal structure of...) |
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| - | [[Image:1rzr.gif|left|200px]]<br /><applet load="1rzr" size=" | + | [[Image:1rzr.gif|left|200px]]<br /><applet load="1rzr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rzr, resolution 2.80Å" /> | caption="1rzr, resolution 2.80Å" /> | ||
'''crystal structure of transcriptional regulator-phosphoprotein-DNA complex'''<br /> | '''crystal structure of transcriptional regulator-phosphoprotein-DNA complex'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Carbon catabolite repression (CCR) is one of the most fundamental | + | Carbon catabolite repression (CCR) is one of the most fundamental environmental-sensing mechanisms in bacteria and imparts competitive advantage by establishing priorities in carbon metabolism. In gram-positive bacteria, the master transcription regulator of CCR is CcpA. CcpA is a LacI-GalR family member that employs, as an allosteric corepressor, the phosphoprotein HPr-Ser46-P, which is formed in glucose-replete conditions. Here we report structures of the Bacillus megaterium apoCcpA and a CcpA-(HPr-Ser46-P)-DNA complex. These structures reveal that HPr-Ser46-P mediates a novel two-component allosteric DNA binding activation mechanism that involves both rotation of the CcpA subdomains and relocation of pivot-point residue Thr61, which leads to juxtaposition of the DNA binding regions permitting "hinge" helix formation in the presence of cognate DNA. The structure of the CcpA-(HPr-Ser46-P)-cre complex also reveals the elegant mechanism by which CcpA family-specific interactions with HPr-Ser46-P residues Ser46-P and His15 partition the high-energy CCR and low-energy PTS pathways, the latter requiring HPr-His15-P. |
==About this Structure== | ==About this Structure== | ||
| - | 1RZR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium] with SO4 and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1RZR is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bacillus_megaterium Bacillus megaterium] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RZR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bacillus megaterium]] | [[Category: Bacillus megaterium]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Allen, G | + | [[Category: Allen, G S.]] |
| - | [[Category: Brennan, R | + | [[Category: Brennan, R G.]] |
| - | [[Category: Schumacher, M | + | [[Category: Schumacher, M A.]] |
[[Category: MG]] | [[Category: MG]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:56:20 2008'' |
Revision as of 12:56, 21 February 2008
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crystal structure of transcriptional regulator-phosphoprotein-DNA complex
Overview
Carbon catabolite repression (CCR) is one of the most fundamental environmental-sensing mechanisms in bacteria and imparts competitive advantage by establishing priorities in carbon metabolism. In gram-positive bacteria, the master transcription regulator of CCR is CcpA. CcpA is a LacI-GalR family member that employs, as an allosteric corepressor, the phosphoprotein HPr-Ser46-P, which is formed in glucose-replete conditions. Here we report structures of the Bacillus megaterium apoCcpA and a CcpA-(HPr-Ser46-P)-DNA complex. These structures reveal that HPr-Ser46-P mediates a novel two-component allosteric DNA binding activation mechanism that involves both rotation of the CcpA subdomains and relocation of pivot-point residue Thr61, which leads to juxtaposition of the DNA binding regions permitting "hinge" helix formation in the presence of cognate DNA. The structure of the CcpA-(HPr-Ser46-P)-cre complex also reveals the elegant mechanism by which CcpA family-specific interactions with HPr-Ser46-P residues Ser46-P and His15 partition the high-energy CCR and low-energy PTS pathways, the latter requiring HPr-His15-P.
About this Structure
1RZR is a Protein complex structure of sequences from Bacillus megaterium with and as ligands. Full crystallographic information is available from OCA.
Reference
Structural basis for allosteric control of the transcription regulator CcpA by the phosphoprotein HPr-Ser46-P., Schumacher MA, Allen GS, Diel M, Seidel G, Hillen W, Brennan RG, Cell. 2004 Sep 17;118(6):731-41. PMID:15369672
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