1sxh

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|PDB= 1sxh |SIZE=350|CAPTION= <scene name='initialview01'>1sxh</scene>, resolution 2.75&Aring;
|PDB= 1sxh |SIZE=350|CAPTION= <scene name='initialview01'>1sxh</scene>, resolution 2.75&Aring;
|SITE=
|SITE=
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|LIGAND=
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|LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= CCpa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 Bacillus megaterium])
|GENE= CCpa ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1404 Bacillus megaterium])
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|DOMAIN=
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|RELATEDENTRY=[[1sxg|1SXG]], [[1sxi|1SXI]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sxh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sxh OCA], [http://www.ebi.ac.uk/pdbsum/1sxh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sxh RCSB]</span>
}}
}}
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[[Category: Schumacher, M A.]]
[[Category: Schumacher, M A.]]
[[Category: Seidel, G.]]
[[Category: Seidel, G.]]
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[[Category: allosterism; phosphoprotein; transcription regulation; gram positive bacteria; ccr]]
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[[Category: allosterism]]
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[[Category: ccr]]
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[[Category: gram positive bacteria]]
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[[Category: phosphoprotein]]
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[[Category: transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:10:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:48:18 2008''

Revision as of 20:48, 30 March 2008


PDB ID 1sxh

Drag the structure with the mouse to rotate
, resolution 2.75Å
Ligands:
Gene: CCpa (Bacillus megaterium)
Related: 1SXG, 1SXI


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



apo structure of B. megaterium transcription regulator


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

1SXH is a Single protein structure of sequence from Bacillus megaterium. 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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